Biochemistry Mnemonics
Dr K Chaudhry

FIRST Author of Jaypee Brothers

 

 

 

 

Credits :-

Dr BC Harinath

Former Dean, MGIMS Wardha

Virtual BRAND AMBASSADOR of My Colorimeter

 

Dr (Brig) MN Chatterjea

Author : Textbook of Medical Biochemistry

 

Godfather of my Colorimeter in CMC Ludhiana & MGM MC Aurangabad

 

Dr Rebecca Abraham

GodMOTHER of my Colorimeter in CMC Ludhiana

 

Dr Rittu Chandel

Author : Postgraduate Biochemistry

 

My Sustained Morale Booster


 

 

 

 

Contents

 

 

Page

01

Introduction

03

02

Enzymes

06

03

Carbohydrates

13

04

Lipids

16

05

Prostaglandins

20

06

Aminoacids & Proteins

21

07

Haemoglobin

29

07

Vitamins & Coenzymes

30

08

Mineral metabolism

31

 


 

 

Chapter 01 : Introduction

 

Principal Methods and Preparations

 

Some

 

A.      Separating and Purifying Biomolecules

 

Same

 

1.    Salt fractionation (eg, precipitation of proteins with ammonium sulfate)

 

Condition

 

2.    Chromatography: Paper, ion exchange, affinity, thin-layer, gas–liquid, high-pressure liquid, gel filtration

 

Every

 

3.    Electrophoresis: Paper, high-voltage, agarose, cellulose acetate, starch gel, polyacrylamide gel, SDSpolyacrylamide gel

 

Unit

 

4.    Ultracentrifugation

Boy

 

B.      Determining Biomolecular Structures

 

Even

 

1.      Elemental analysis

 

Unknown

 

2.    UV, visible, infrared, and NMR spectroscopy

 

Unheard

 

3.    Use of acid or alkaline hydrolysis to degrade the biomolecule under study into its basic constituents

 

Urologist

 

4.       Use of a battery of enzymes of known specificity to degrade the biomolecule under study (eg, proteases, nucleases, glycosidases)

 

May

 

5.    Mass spectrometry

 

See

 

6.    Specific sequencing methods (eg, for proteins and nucleic acids)

 

X-ray

 

7.      X-ray crystallography

Stole

 

C.      Studying Biochemical Processes

 

Women

 

1.      Whole animal (includes transgenic animals and animals with gene knockouts)

 

In

 

2.      Isolated perfused organ

 

Turkey

 

3.      Tissue slice

 

With

 

4.      Whole cells

 

Husbands

 

5.      Homogenate

 

In

 

6.      Isolated cell organelles

 

Spain

 

7.      Subfractionation of organelles

 

Preaching

 

8.      Purified metabolites and enzymes

 

Intensely

 

9.      Isolated genes (including polymerase chain reaction and site-directed mutagenesis

 

Major Causes of Diseases

People

 

1. Physical agents

 

Many

 

Mechanical trauma

 

Employees

 

Extremes of temperature

 

Spoil

 

Sudden changes in atmospheric pressure

 

Remaining

 

Radiation

 

Employees

 

Electric shock

Can

 

2. Chemical agents, including drugs

 

 

 

Certain toxic compounds

 

 

 

Therapeutic drugs

Buy

 

3. Biologic agents

 

Visiting

 

Viruses

 

Boy

 

Bacteria

 

From

 

Fungi

 

Hapur

 

Higher forms of parasites

Only

 

4. Oxygen lack

 

Let

 

Loss of blood supply

 

People

 

Depletion of the oxygen-carrying capacity of the blood

 

Play

 

Poisoning of the oxidative enzymes

Gold

 

5. Genetic disorders

 

 

 

Congenital

 

 

 

Molecular

In

 

6. Immunologic reactions

 

 

 

Anaphylaxis

 

 

 

Autoimmune disease

North

 

7. Nutritional imbalances

 

 

 

Deficiencies

 

 

 

Excesses

East

 

8. Endocrine imbalances

 

 

 

Hormonal deficiencies

 

 

 

Hormonal excesses

 


 Causes of diseases

P

Physical agents

 

 

 

Mechanical trauma

 

 

Temperature extremes

 

 

Atmospheric pressure

 

 

Radiation

 

 

Electric shock

C

Chemical agents

 

 

 

Drugs

 

 

Toxic compounds

B

Biological agents

 

 

 

Viruses

 

 

Bacteria

 

 

Fungi

 

 

Parasites

H

Hypoxaemia

 

 

 

Ischaemia

 

 

Haemoglobinopathies

 

 

Poisoning

G

Genetic disorders

 

 

 

Congenital

 

 

Molecular

I

Immunological reactions

 

 

 

Anaphylaxis

 

 

Autoimmune disease

N

Nutritional imbalances

 

E

Endocrine imbalances

 

Chromatography

Central

Column chromatography

Pay

Partition chromatography

Scales

Size exclusion chromatography

Are

Absorption chromatography

In

Ion exchange chromatography

Huge

Hydrophobic interaction chromatography

Acceptance

Affinity chromatography

 

Organelle of Eukaryote Cell

 

N

 

1. Nucleus

 

No

 

(i)                 Nuclear envelope

 

Nurse

 

(ii)               Nuclear pore complexes

 

Can

 

(iii)             Chromatin

 

Nurse

 

(iv)             Nucleolus

 

Negligently

 

(v)               Nucleoplasm

M

 

2. Mitochondrion: 2 Mitochondrial Membranes

 

Only

 

(a) Outer mitochondrial membrane

 

Indians

 

 (b) Inner mitochondrial membrane

 

In

 

(c) Intermembrane space

 

Meeting

 

 (d) Mitochondrial matrix

E

 

3. Endoplasmic reticulum (ER)

 

 

 

 (i) Rough surfaced ER

 

 

 

 (ii) Smooth surfaced ER

G

 

4. Golgi complexes or Golgi apparatus or Dictyosomes

 

Pre

 

(i)                 Proximal or Cis compartment,

 

Marital

 

(ii)               Medial compartment

 

Depression

 

(iii)             Distal or trans compartment.

 

 

 

 

L

 

5. Lysosomes

P

 

6. Peroxisomes

C

 

7. Cytoskeleton

 

M

 

(a) Microtubules

 

M

 

(b) Microfilaments

 

M [3 Masters]

 

(c) Microtrabeculae

 

 

Organelle of Plant Cell

 

Come

1.       Chloroplasts

Guys

2.       Glyoxisomes

Consume

3.       Cell wall

Vodka

4.       Vacuole

 

 

Lysosomal Enzymes

 

 

P

 

1. Proteolytic enzymes

 

Can

 

Cathepsins (Proteinase)

 

Come

 

Collagenase

 

Easily

 

Elastase

N

 

2. Nucleic acid hydrolysing enzymes

 

 

 

Ribonucleases

 

 

 

Deoxyribonucleases

L

 

3. Lipid hydrolysing

 

Let

 

Lipases enzymes

 

People

 

Phospholipases

 

Find

 

Fatty acyl esterases

C

 

4. Carbohydrate

 

A

 

α-glucosidase splitting enzymes

 

B

 

β-galactosidase

 

H

 

Hyaluronidase

 

A [Abha]

 

Aryl sulphatase, etc.

O

 

5. Other enzymes

 

 

 

Acid phosphatase

 

 

 

Catalase, etc.

 

Biological membranes

 

Passion

1.      Plasma membrane (mammals)

Never

2.      Nuclear membrane

Occurs

3.      Outer mitochondrial membrane

In

4.      Inner mitochondrial membrane

Every

5.      Endoplasmic reticulum

Man

6.      Myelin

 

Chemical Composition of the Membranes

 

Let

 

(a) Lipids

 

 

Few

 

1. Fatty acids

 

 

Guys

 

2. Glycerophospholipids

 

 

 

 

Phosphatidylethanolamine (cephalin)

 

 

 

 

Phosphatidylcholine (Lecithin)

 

 

 

 

Phosphatidylserine

 

Spend

 

3. Sphingolipids

 

 

 

 

Sphingomyelin

 

 

 

 

Cerebrosides

 

 

 

 

Gangliosides

 

Cents

 

4. Cholesterol

Public

 

 (b) Proteins

 

I

 

1. Integral membrane proteins (intrinsic membrane proteins)

 

Paid

 

2. Peripheral membrane proteins (extrinsic proteins)

 

Them

 

3. Transmembrane proteins

Come

 

 (c) Carbohydrates

 

 

 

 

Concanavalin

 

 

 

 

Glycophorin

Daily

 

(d) Additional Special Features

 

 

 

 

(a) Lipid rafts

 

 

 

 

(b) Caveolae

 

Special Structural Characteristics of Red Cells Membranes

 

1. Integral proteins

 

 

 (a) Glycophorin and

 

 

(b) Band-3-Protein.

 

2. Peripheral proteins

 

 

Spectrin

 

 

Actin

 

 

Ankyrin

 

Transport Systems

India

1. Ion Channels

 

 

a. Ligand gated channels

 

 

b. Voltage gated channels

Is

2. Ionophores

 

 

(a) Mobile ion carriers

 

 

(b) Channel formers

Winning

3. Water Channels (Aquaporins)

Gold

4. Gap Junction

 

Types of Transport Mechanisms

 

 (a) Passive or simple diffusion

 

 

Water

 

 

Gases

 

 

Pentose sugars

 

 (b) Facilitated diffusion

 

 

D-fructose absorbed from intestine

 

(c) Active transport

 

Factors affecting net diffusion

 

Can

1.      Concentration gradient

Easily

2.      Electrical potential

Handle

3.      Hydrostatic pressure gradient

Two

4.      Temperature

Parties

5.      Permeability coefficient

 

Transport of Macromolecules

 

1. Exocytosis

 

 

 (i) Can attach to the cell surface and become peripheral proteins, e.g. antigens.

 

 

(ii) They can become part of extracellular matrix, e.g. collagen and glycosaminoglycans (GAGs)

 

 

(iii) Hormones like insulin, parathormone (PTH) and catecholamines

 

2. Endocytosis

 

 

(i) Phagocytosis

 

 

(ii) Pinocytosis

 

 

 

(a) Fluid phase pinocytosis

 

 

 

(b) Receptor mediated absorptive pinocytosis


 

Chapter 02 : Enzymes

 

Properties of Enzyme

 

A

Active site - Special pocket or cleft present in Enzyme

Caring

Catalytic efficiency/ Enzyme turnover number

S

Specificity

R

Regulation

Z

Zymogens - inactive form of enzyme

I

Isoenzymes (Isozymes)

 

Class of Enzymes

On

 

Class I. Oxidoreducatases

 

A

 

Alcohol dehydrogenase,

 

Lung

 

Lactate dehydrogenase

 

X-ray

 

Xanthine oxidase

 

Gaining

 

Glutathione reductase,

 

Great

 

Glucose-6-phosphate dehydrogenase

Tuesday

 

Class II. Transferases

 

An

 

Aspartate  transaminase (AST)

 

Anchor

 

Alanine  transaminase (ALT)

 

Has

 

Hexokinase

 

Played

 

Phosphoglucomutase

 

His

 

Hexose-1-phosphate

 

Unique

 

Uridyltransferase

 

Organ

 

Ornithine carbamoyl transferase

He

 

Class III. Hydrolases

Left

 

Class IV. Lyases

 

Failed

 

Fumarase

 

And

 

Arginosuccinase

 

Harassed

 

Histidine decarboxylase

In

 

Class V. Isomerases

 

Universe

 

UDP-glucose

 

Entering

 

Epimerase

 

Really

 

Retinal isomerase

 

Rattling

 

Racemases

 

Time

 

Triosephosphate isomerase

Lorry

 

Class VI. Ligases or synthetases

 

A

 

Alanyl-t. RNA synthetase

 

Game

 

Glutamine synthetase

 

Drain

 

DNA ligases

 

Regulation of enzyme activity

 

I

1. Irreversible covalent Activation / Zymogen activation

Run

2. Reversible Covalent Modification

And

3. Allosteric Modulation

Flee

4. Feedback inhibition

 

Common enzyme estimations

 

Lift

Lipase

 

And

α- Amylase

 

Then

Trypsin

 

Add

Alkaline phosphates (ALP)

 

Are

Acid Phosphatase (ACP)

 

The

Transaminases

 

 

GOT

 

 

GPT

Laudable

Lactate Dehydrogenase (LDH)

Combo

Creatine kinase (CK) or ceratin phosphokinase (CPK)

 

Classification of Coenzymes

 

 

 (a) For transfer of groups other than hydrogen

S

 

Sugar phosphates,

C

 

CoASH

T

 

Thiamine pyrophosphate (TPP)

P

 

Pyridoxal phosphate

F

 

Folate coenzymes

B

 

Biotin

C

 

Cobamide coenzyme

L

 

Lipoic acid

 

(b) For transfer of hydrogen

N

 

NAD+, NADP+

F

 

FMN, FAD

L

 

Lipoic acid

C

 

Coenzyme Q.

 

Metalloenzymes (Metal Enzymes)

 

 

Copper

 

 

Superoxide dismutase

 

 

Cytochrome oxidase,

 

 

Tyrosinase

 

 

Lysyl oxidase.

 

Calcium

 

 

Lipase

 

 

Lecithinase

 

Iron

 

 

Catalase

 

 

Xanthine oxidase

 

 

Peroxidase cytochrome oxidase.

 

Manganese

 

 

Hexokinase

 

 

Enolase

 

 

Phosphoglucomutase

 

 

Glycosyl transferase

 

Magnesium

 

 

Hexokinase

 

 

Enolase, glucose-6-phosphatase,

 

 

phosphofructokinase

 

Molybdenum

 

 

Xanthine oxidase

 

Zinc

 

 

Carbonic anhydrase

 

 

Alcohol dehydrogenase,

 

 

Carboxy peptidase

 

 

Alkaline phosphatase (ALP),

 

 

Lactate dehydrogenase (LDH).

 

Specificity of enzymes

Some

Stereochemical specificity

Are

Absolute specificity

Great

Group dependent or

Leaders

Linkage Specificity

 

Factors affecting enzyme action

 

T

1. Temperature

P

2. pH

E

3. Enzyme Concentration

P

4. Product Concentration

S

5. Substrate Concentration

A

6. Activators and Coenzymes

M

7. Modulators and Inhibitors

T

8. Time

 

Enzyme inhibition

Can

 

1. Competitive Inhibition

 

 

A

 

Allopurinol

 

S

 

Sulphonamides

 

M

 

Methotrexate

 

M

 

MAO inhibitors

 

P

 

Physostigmine

 

D

 

Dicoumarol

 

S

 

Succinylcholine

Never

 

2. Non-competitive Inhibition

 

 

 

 

 (i) reversible

 

 

 

(ii) irreversible

 

I

 

 

Iodoacetate

 

H

 

 

Heavy metal ions

 

F

 

 

Fluoride

 

B

 

 

BAL (British anti Lewesite)

 

D

 

 

Disulfiram (Antabuse)

 

D

 

 

Di-isopropyl fluorophosphate (DFP)

 

S

 

 

Suicide Inhibition

 

 

 

 

 

Allopurinol

 

 

 

 

 

Aspirin

 

 

 

 

 

5-fluorouracil

Attack

 

3. Allosteric Inhibition and Allosteric Enzymes

 

 

 

 

Ubiquitin

 

 

 

 

Ubiquitination

 


 

 

Chapter 03 : Carbohydrates

 

Sugars with corresponding alcohol

 

Girl

Glucose

Sorbitol

From

Fructose

Sorbitol and mannitol

Madras

Mannose

Mannitol

Gazing

Glyceraldehyde

Glycerol

Every

Erythrose

Erythritol

Entry

Ribose

Ribitol

Gate

Galactose

Dulci tol

 

Carbohydrates - Classification

 

1. Monosaccharides

 

 

Trioses

 

 

 

Glyceraldehyde

 

 

 

Dihydroxyacetone

 

 

Tetroses

 

 

 

 

Erythrose

 

 

 

Erythrulose

 

 

Pentoses

 

 

 

Ribose

 

 

 

Ribulose

 

 

Hexoses

 

 

 

Glucose

 

 

 

Fructose

 

2. Disaccharide

 

 

Maltose

 

 

 

Lactose

 

 

 

Sucrose

 

 

 

Lactulose

 

 

3. Oligosaccharides

 

4. Polysaccharides (Glycans)

 

 

a. Homopolysaccharides (homoglycans

 

 

 

Starch

 

 

 

Glycogen

 

 

 

Inulin

 

 

 

Cellulose

 

 

 

Dextrins

 

 

 

Dextrans

 

 

b. Heteropolysaccharides (heteroglycans)

 

 

 

Mucopolysaccharides (glycosaminoglycans)

 

General Properties

A

Asymmetric carbon

V

Van’t Hoff’s rule of ‘n’

S

Stereoisomerism

D

D-Series and L-Series

O

Optical activity

 

Properties of Monosaccharides

 

In

1. Iodocompounds

 

An

2. Acetylation or ester formation

 

Open

3. Osazone formation

 

Indoor

4. Interconversion of sugars

 

Opera

5. Oxidation to produce sugar acids

 

 

(i) Aldonic acids

 

 

(ii) Saccharic or aldaric acid

 

 

(iii) Uronic acids

Raids

6. Reduction of sugars to form sugar alcohols

Are

7. Action of acids on carbohydrates

 

Always

8. Action with alkalies

 

 

(a) In dilute alkali

 

 

(b) In conc. alkali

Rare

9. Reducing action of sugars in alkaline solution

 

Mucopolysaccharides (MPS) - Classification

A

 

I. Acidic Sulphate free MPS

 

 

 

1. Hyaluronic Acid

 

 

 

2. Chondroitin

S

 

II. Sulphate Containing Acid MPS

 

Korean

 

1. Keratan Sulphate (Kerato Sulphate)

 

 

 

 

a.       Keratan SO4 I

 

 

 

 

b.      Keratan SO4 II

 

Cheats

 

2. Chondroitin Sulphates

 

 

 

 

a. Chondroitin SO4 A

 

 

 

 

b. Chondroitin SO4 B

 

 

 

 

c. Chondroitin SO4 C

 

 

 

 

d. Chondroitin SO4 D

 

Have

 

3. Heparin

 

Hacked

 

4. Heparitin Sulphate

N

 

III. Neutral MPS

 

 

 

a.       Blood group substances

 

 

 

b.      Nitrogenous neutral MPS

 

Naturally occurring thrombin inhibitors in plasma :

A

Antithrombin III

Monkey

2-Macroglobulin

Has

Heparin cofactor II

Attacked

1-Antitrypsin

 

Functions of Proteoglycans

 

 

1.      As a constituent of extracellular matrix or ground substance

 

2.      Acts as polyanions

 

3.      Acts as a barrier in tissue

 

4.      Acts as lubricant in joints

 

5.      Role in release of hormone

 

6.      Role in cell migration in embryonic tissues

 

7.      Role in glomerular filtration

 

8.      Role as anticoagulant in vitro and in vivo:

 

9.      Role as a coenzyme

 

10.  As a receptor of cell

 

11.  Role in compressibility of cartilages

 

12.  Role in sclera of eye

 

13.  Role in corneal transparency


 

 

 

Chapter 04 : Lipids

 

Classification of Lipids

S

 

I. Simple Lipids

 

 

 

 (a) Neutral fats (Triacylglycerol, TG)

 

 

 

 (b) Waxes

 

The

 

 

True waxes

 

Casual

 

 

Cholesterol esters

 

Visit

 

 

Vit A and Vit D esters

C

 

II. Compound Lipids

 

Post

 

 (a) Phospholipids

 

Graduate

 

 (b) Glycolipids

 

Students

 

 (c) Sulpholipids

 

At

 

 (d) Aminolipids (Proteolipids)

 

Loss

 

(e) Lipoproteins

D

 

III. Derived Lipids

 

Feed

 

 (a) Fatty acids

 

Me

 

(b) Monoglycerides (Monoacylglycerol) and Diglycerides

 

Apple

 

 (c) Alcohols

M

 

IV. Miscellaneous

 

A

 

 

Aliphatic hydrocarbons

 

Casual

 

 

Carotenoids

 

Solitary

 

 

Squalene

 

Visitor

 

 

Vitamins E and K.

 

TYPES OF FATTY ACIDS

 

Some

(a) Saturated FA

 

 

 

Acetic acid CH3COOH

 

 

 

Propionic acid C2H5COOH

 

 

 

Butyric acid C3H7COOH

 

 

 

Caproic acid C5H11COOH

 

 

 

Palmitic acid C15 H31COOH

 

 

 

Stearic acid C17 H35COOH

 

Uunmanned

 (b) Unsaturated FA

 

 

 

 (1) Mono unsaturated (Monoethenoid) fatty acids

 

 

 

 (2) Polyunsaturated (Polyethenoid) fatty acids

 

 

 

Linoleic acid series (18 : 2; 9, 12)

 

 

 

Linolenic acid series (18 : 3; 9, 12, 15)

 

 

 

Arachidonic acid series (20 : 4; 5, 8, 11, 14)

Boy

 (c) Branched chain FA

Sent

 (d) Substituted fatty acids

 

Cracked

 (e) Cyclic fatty acids

 

 

 

Chaulmoogric acid

 

 

 

Hydnocarpic acid

 

Eggs

 (f) Eicosanoids

 

 

Essential fatty acids (EFA)

 

Laughing

Linoleic acid

Loud

Linolenic acid

Always

Arachidonic acid

 

Functions of EFA: (Biomedical Importance)

 

Structural elements of tissues

 

Structural element of gonads

 

Synthesis of prostaglandins and other compounds

 

Structural element of mitochondrial membrane

 

Serum level of cholesterol

 

Effect on clotting time

 

Effect on fibrinolytic activity

 

Role of EFA in fatty liver

 

Role in vision

 

Deficiency manifestations of EFA

 

Can

Cessation of growth.

See

Skin lesions: Acanthosis (hypertrophy of prickle

A

Abnormalities of pregnancy and lactation in adult

Fast

Fatty liver accompanied by increased rates of

Kite

Kidney damage.

 

Unsaturated Alcohols

 

Principal

 (a) Phytol (Phytyl alcohol)

Leaves

(b) Lycophyll

College

 (c) Carotene

Secretly

 (d) Sphingosine or sphingol

 

Chemical constants of Fats and Oils

 

Send

1. Saponification Number

A

2. Acid Number

Pulse

3. Polenske Number

Recorder

4. Reichert-Meissl Number

In

5. Iodine Number

Ambulance

6. Acetyl Number

 

Types of Phospholipases

 

Phospholipase ‘A’

 

Phospholipase ‘B’

 

Phospholipase ‘C’

 

Phospholipase ‘D’

 

Classification of Phospholipids

 

Good

 

Glycerophosphatides

People

 

Phosphoinositides

Pray

 

Phosphosphingosides

Often

 

Other Phospholipids

 

P

 

1. Phosphatidyl Ethanolamine (Cephalins)

 

P

 

2. Phosphatidyl Inositol (Lipositols)

 

P

 

3. Phosphatidyl Serine

 

L

 

4. Lysophosphatides

 

P

 

5. Plasmalogens

 

S

 

6. Sphingomyelins (phosphatidyl sphingosides)

 

P

 

7. Phosphatidic Acid and Phosphatidyl Glycerol

 

C

 

8. Cardiolipin

 

 

Functions of Phospholipids

 

S

Structural

E

Role in enzyme action

B

Role in blood coagulation

L

Role in lipid absorption in intestine

T

Role in transport of lipids from intestines

T

Role in transport of lipids from liver

E

Role in electron transport

L

Lipotropic action of lecithin

I

Ion transport and secretion

 

GLYCOLIPIDS

C

 

1. Cerebrosides (glycosphingosides)

 

Kanput

 

Kerasin

 

Colleges

 

Cerebron (Phrenosin)

 

Now

 

Nervon

 

Open

 

Oxynervon

G

 

2. Gangliosides

 

 

 

GM-1

 

 

 

GM-2

 

 

 

GM-3

 

 

 

GD-3

S

 

3. Sulpholipids


 

 

Chapter 05 : Prostaglandins

 

Classification

 

 

A.  Prostanoids (PGs), and

 

 

1. Prostaglandins (PGs)

 

 

 

(a) PG-E group: PGE-1, PGE-2 and PGE 3

 

 

 

(b) PG-F group: PGF1á, PGF2á and PGF3á

 

 

 

 (c) PG-A group: PG-A1, PG-A2, 19-OH PG-A1, 19-OH

 

 

 

 (d) PG-B group: PG-B1, PG-B2, 19-OH PG-B1

 

 

2. Prostacyclins (PGI)

 

 

3. Thromboxanes (Tx)

 

 B. Leucotrienes (LT’s) and Lipoxins (Lxs)


 

Chapter 06 : Aminoacids & Proteins

 

Amino acids

 

 

A. Neutral amino acids

 

 

 (a) Aliphatic Amino Acids

 

 

 

1. Glycine (Gly) or α-amino acetic acid.

 

 

 

2. Alanine (Ala) or α-amino propionic acid.

 

 

 

3. Valine (Val) or α-amino-isovaleric acid.

 

 

 

4. Leucine (Leu) or α-amino-isocaproic acid.

 

 

 

5. Isoleucine (Ile) or α-amino- β-methyl valeric acid.

 

 

 

6. Serine (Ser) or α-amino-β-hydroxy propionic acid.

 

 

 

7. Threonine (Thr) or α-amino-β-hydroxybutyric acid.

 

 

(b) Aromatic Amino Acids

 

 

 

8. Phenylalanine (Phe) or α-amino-β-phenyl propionic acid.

 

 

 

9. Tyrosine (Tyr) or parahydroxy phenylalanine

 

 

 (c) Heterocyclic Amino Acids

 

 

 

10. Tryptophan (Trp) or α-amino-β-3-indole propionic acid.

 

 

 

11. Histidine (His) or α-amino-β-imidazole propionic acid

 

 

 (d) Imino Acids

 

 

 

12. Proline (Pro) or Pyrrolidone-2-carboxylic acid.

 

 

 

13. Hydroxyproline (Hyp) or 4 hydroxy pyrrolidone-2 carboxylic acid.

 

 

 (e) ‘S’ containing amino acids

 

 

 

14. Cysteine (Cys) or α-amino-β-mercaptopropionic acid.

 

 

 

15. Methionine (Met) or α-amino-¡-methylthio-h-butyric acid

 

B. Acidic amino acids

 

 

 

16. Aspartic acid (Asp) or α-amino succinic acid.

 

 

 

17. Glutamic Acid (Glu) or α-aminoglutaric acid.

 

C. Basic amino acids

 

 

 

18. Arginine (Arg) or α-amino-d-guanidino-n-valeric acid.

 

 

 

19. Lysine (Lys) or α- å-diamino caproic acid.

 

 

 

20. Hydroxylysine (Hyl) or α- å-diamino-d-hydroxy-nvaleric acid.

 

New Amino Acids

 

A. Selenocysteine - 21st amino acids

 

B. Pyrrolysine - 22nd amino acid

 

 

Non-standard Amino Acids

 

A.     Non-protein amino acid structure s

 

 

β-alanine

 

 

Taurine

 

 

Ornithine and citrulline

 

 

Thyroxine (T4) and Tri-iodo Thyronine (T3)

 

 

¡-aminobutyric acid (GABA)

 

 

β-amino isobutyric acid

 

 

d-aminolaevulinic acid (-ALA)

 

 

S-adenosyl methionine (SAM)

 

 

3, 4-dihydroxy phenyl alanine (DOPA)

 

B.     D-amino acids

 

 

D-glutamic acid and D-Alanine

 

 

D-amino acids

 

Nutritional Classification

 

Express

 (a) Essential amino acids – Not synthesized in body

News

 (b) Non-essential amino acids – Synthesized in body

Service

 (c) Semi-essential amino acids – Synthesized in body in inadequate quantity

 

Properties of amino acids

I

A. Isomerism

 

 

 

 (a) Stereoisomerism

 

 

 

 (b) Optical Isomerism

A

B. Amphoteric Nature and Isoelectric pH

P

C. Physical Properties:

 

 

 

Colourless,

 

 

 

Crystalline

 

 

 

More soluble in water than in polar solvents.

 

 

 

High melting point usually more than 200°C

 

 

 

High dielectric constant

 

 

 

Large dipole moment

D

D. Chemical Properties

 

 

I. Due to Carboxylic (—COOH) Group

 

 

 

1. Formation of esters

 

 

 

2. Reduction to amino alcohol

 

 

 

3. Formation of amines by decarboxylation

 

 

 

4. Formation of amides

 

 

II. Properties Due to Amino (–NH2) Group

 

 

 

1. Salt formation with acids

 

 

 

2. Formation of acyl derivatives

 

 

 

3. Oxidation

 

 

 

4. Reaction with HNO2

 

 

 

5. Reaction with CO2

 

 

 

6. Reaction with formaldehyde

 

 

 

7. Specific colour reactions

 

 

III. Properties of Amino acids Due to Both NH2 and COOH Groups

 

Classification of proteins - On the basis of shape and size

 

Fibrous proteins

 

 

Keratin from hair

 

 

Collagen.

 

Globular protein

 

 

Myoglobin,

 

 

Haemoglobin,

 

 

Ribonuclease

 

Classification of proteins - On the basis of functional properties

 

D

Defence proteins

 

 

 Immunoglobulins involved in defence mechanisms.

C

Contractile proteins:

 

 

Proteins of skeletal muscle involved in muscle contraction and relaxation.

R

Respiratory proteins

 

 

Haemoglobin,

 

 

Myoglobin,

 

 

Cytochromes.

S

Structural proteins:

 

 

 Proteins of skin, cartilage, nail.

E

Enzymes: Proteins acting as enzymes.

H

Hormones: Proteins acting as hormones.

 

Classification of proteins - On the basis of solubility and physical properties

 

 

A. Simple Proteins

 

 

1. Protamines

 

 

 

Salmine

 

 

 

Sardinine

 

 

 

cyprinine of fish sperms and testes.

 

 

2. Histones

 

 

 

Nucleohistones,

 

 

 

chromosomal nucleoproteins

 

 

 

globin of haemoglobin.

 

 

3. Albumins

 

 

 

Plant albumins:

 

 

 

Legumelin in legumes,

 

 

 

Leucosin in cereals.

 

 

 

Animal source:

 

 

 

Ovalbumin in egg,

 

 

 

lactalbumin in milk.

 

 

4. Globulins

 

 

 

Hemopexin

 

 

 

Transferrin

 

 

 

Ceruloplasmin

 

 

 

immunoglobulins.

 

 

 

ovoglobulin in eggs,

 

 

 

lactoglobulin in milk

 

 

 

legumin from legumes.

 

 

5. Gliadins (Prolamines)

 

 

 

Gliadin of wheat

 

 

 

hordein of barley.

 

 

6. Glutelins

 

 

 

Oryzenin of rice

 

 

 

glutelin of wheat.

 

 

7. Scleroproteins or Albuminoids

 

 

 

 (a) Keratins

 

 

 

 (b) Collagen

 

 

 

Gelatin

 

 

 

 (c) Elastins

 

B. Conjugated Proteins

 

 

1. Nucleoproteins

 

 

 

(i) Deoxyribonucleoproteins

 

 

 

(ii) Ribonucleoproteins

 

 

 

Nucleohistone

 

 

 

b. nucleoprotamine.

 

 

2. Mucoproteins or Mucoids

 

 

3. Glycoproteins

 

 

4. Chromoproteins

 

 

 

 (a) Haemoproteins

 

 

 

• Haemoglobin

 

 

 

• Cytochromes

 

 

 

• Catalase

 

 

 

• Peroxidase

 

 

 

(b) Others

 

 

 

• Flavoprotein

 

 

 

• Visual purple

 

 

5. Phosphoproteins

 

 

6. Lipoproteins

 

 

7. Metalloproteins

 

 

 

Ferritin

 

 

 

Carbonic Anhydrase

 

 

 

Ceruloplasmin

 

C. Derived Proteins

 

 

 (a) Primary derived proteins

 

 

1. Proteans

 

 

 

Myosan

 

 

 

Edestan

 

 

 

Fibrin

 

 

2. Metaproteins

 

 

3. Coagulated proteins

 

 

 

cooked meat protein

 

 

 

cooked egg albumin protein

 

 

 

alcohol precipitated protein

 

 

(b) Secondary derived proteins

 

 

1. Proteoses or albumoses

 

 

2. Peptones

 

 

3. Peptides

 

 

 

Dipeptides

 

 

 

Tripeptides

 

 

Biologically Important Peptides

 

G

Glutathione

C

Carnosine

B

Bradykinin

O

Oxytocin and Vasopressin

A

Angiotensins

G

Gastrin, Secretin and Pancreozymin

C

β-Corticotropin (ACTH), and β MSH

A

Antibiotics

B

Brain Peptides

 

Normal values of plasma proteins

 

Total Proteins = 7.0 to 7.5 Gm%

 

By Precipitation

(Gm %)

By Paper Electrophoresis

(% of total proteins)

Albumin

3.7-5.2

50-70

Globulins

1.8-3.6

29.5-54

α1-globulin

0.1-0.4

2.0-6.0

α2-globulin

0.4-0.8

5.0-11.0

β-globulin

0.5-1.2

7.0-16.0

¡-globulin

0.7-1.5

11.0-22.0

Fibrinogen

0.2-0.4

 

A:G ratio = 2.5:1.0 to 1.2:1.0 (Mode : 2:1)

 

 

Electrophoretic Pattern in different diseases

 

Disease

Alb

α1-glo

α2-glo

β-glo

¡-glo

Nephrosis

down

 

up

 

down

Chronic liver disease

 

 

 

 

Up

Infective hepatitis

 

down

down

 

Up

Diabetes mellitus

 

 

up

 

 

Rheumatoid arthritis

 

 

 

up

Up

Systemic lupus erythematosus

 

 

 

up

up

Sarcoidosis

 

 

up

up

up

Lymphatic leukaemia

 

 

 

 

down

Myelogenous and monocytic leukaemia

 

 

 

 

up

Multiple myeloma

Sharp paraprotein band in β to ¡-region (M band-monoclonal)

 

Acute Phase Proteins (or Reactants)

C

C-reactive protein (CRP)

H

Haptoglobin (Hp)

A

α1-Antitrypsin

A

α1-Acid glycoprotein (orosomucoid) and

F

Fibrinogen

 

Proteins excreted in urine may be of following types:-

 

Send

Serum albumin

A

Albumoses

Paper

Peptones

Boat

Bence-Jones proteins.

 

Causes of Hypoproteinaemia
 

Kidney disorders

Massive proteinuria, nephrotic syndrome

Intestinal disorders

Idiopathic exudative enteropathy, enteritis, colitis, fistulae, amyloidosis, polyadenomatosis, Whipple's disease, lymph node metastases

Skin conditions

Burns, Exudative dermatosis

Malnutrition

 

Proteinuria - Functional or physiological

Please

(i) Postural or orthostatic 

Examine

(ii) Exertion

My

(iii) Mental strain

Papa

(iv) Prolonged exposure to cold 

Paying

(v) Pregnancy and premenstrual period 

Fee

(vi) First week of neonatal period

Proteinuria – Pre-renal causes

Can

(a) Cardiac decompensation

Faculty

(b) Fever

Trainer

(c)  Toxemia

Advise

(d)  Ascites and intraabdominal tumours

Healthy

(e)  Heavy metals, e.g., bismuth, mercury

Diet

(f)  Drugs, e.g., salicylic acid

Proteinuria – Renal causes

China

(a) Chronic glomerulonephritis 

Never

(b) Nephrotic syndrome

Resists

(c) Renal tuberculosis

Indian

(d) Infarction of the kidney

Military

(e) Malignancy

 
 

Proteinuria – Post-renal causes

Primary

(a) Pyelitis

Care

(b) Cystitis

Unit

(c) Urethritis

 

Bence-Jones Proteins present in :

My

(i) Multiple myeloma

Son

(ii) Sarcomatosis

Has

(iii) Hypernephroma

Low

(iv) Leukemia

Backache

(v) Bronchogenic carcinoma

 

CSF Proteins


Normal 20-30 mg/100 ml.

 

Raised in

 

My

 

(a) Meningitis

Enemies

 

(b) Encephalitis

Not

 

(c) Neurosyphilis

Coming

 

(d) Cerebral arteriosclerosis

 

Cyto-albumin dissociation seen in

Post

 

(a) Poliomyelitis (early stage)

Natal

 

(b) Neurosyphilis

Depression

 

(c) Disseminated sclerosis

 

Caeruloplasmin - Clinical Importance

 

 

Increase

Pain

 

Pregnancy

In

 

Inflammatory processes

My

 

Malignancies

Own

 

Oral oestrogen therapy

Chest

 

 Contraceptive pills.

 

Decrease

 

 

Wilson’s disease

 

 

Menke’s disease

 

Plasma Transferrin increased in :

 

Please

(i) Pregnancy

Do

(ii) Diabetes mellitus

Deliver

(iii) Duchenne muscular dystrophy

Medicines

(iv) Malignancies - Melanomas.

 

α2-Globulins

 

 

1. Caeruloplasmin

 

2. Haptoglobin

 

β-Globulins

 

Leave

1. β-Lipoproteins (LDL)

Travel

2. Transferrin

Concession

3. C-reactive Protein

Has

4. Haemopexin

Commenced

5. Complement C1q

 

Genetic deficiencies of plasma proteins

 

A

1. Analbuminaemia

B

2. Bisalbuminaemia

B

3. Bruton’s agammaglobulinaemia

A [Abba]

4. Afibrinogenaemia


Chapter 07 : Haemoglobin

 

Normal human haemoglobin

 

 

1. Hb-A1

 

2. Hb-F

 

3. Hb-A2

 

4. Embryonic Hb

 

5. Hb-A3

 

6. Hb-A1C (Glycosylated Hb)

 

Derivatives of haemoglobin

 

1.      Haematins

 

 

Acid haematin

 

 

Alkali haematin

 

2. Haemin

 

3. Haemochromogen

 

 

4. Haematoporphyrin

 

 

5. Haematoidin

 

 

6. Methaemoglobin

 

 

7. Methaemalbumin

 

 

Gas derivatives

 

One

1. Oxyhaemoglobin

Counting

2. Carboxyhaemoglobin

Chamber

3. Carbaminohaemoglobin

Stored

4. Sulfhaemoglobin

Carefully

5.- Cyanmethaemoglobin

 

Haemoglobinopathies

 

1. Hb-S

 

2. Hb-M

 

3. Hb-Sabine

 

4. Hb-Chesapeake

 

5. Hb-Rainier

 

6. Hb-Constant Spring

 

Other abnormal haemoglobins

 

 

Hb-C

 

 

Hb-D (Panjab)

 

 

Hb-E


 

Chapter 08 : Vitamins & Coenzymes

Classification

 

 

1. Fat-soluble Vitamins

 

 

 

Vitamin A

 

 

 

Vitamin D

 

 

 

Vitamin E, and

 

 

 

Vitamin K.

 

2. Water-soluble Vitamins

 

 

(a) Vitamin C (ascorbic acid),

 

 

(b) Vitamin B complex

 

 

 

Vitamin B1 (thiamine)

 

 

 

Vitamin B2 (riboflavin)

 

 

 

Niacin (nicotinic acid)

 

 

 

Vitamin B6 (pyridoxine)

 

 

 

Pantothenic acid

 

 

 

α-Lipoic acid

 

 

 

Biotin

 

 

 

Folic acid group

 

 

 

Vitamin B12 (cyanocobalamine).

 

 

 

Inositol

 

 

 

Para-amino benzoic acid (PABA)

 

 

 

Choline.

 

B – Vitamins

 

The

1.    Thiamine (Vit B1)

Rogues

2.      Riboflavin (Vit B2 )

Never

3.    Niacin (Nicotinic acid (or Nicotinamide)

Pounce

4.    Pantothenic acid (Vit B5)

Very

5.    Vitamin B6 (Pyrodoxine,pyridoxal,& Pyridoxamine)

Brutally

6.    Biotin

Visiting

7.    Vitamin B12 (Cobalamin)

Family

8.      Folic Acid

 

Functions of Vitamins

 

Come

Collagen biosynthesis

Darling

Degradation of Tyrosine

And

Absorption of Iron

Sit

Steroidogenesis

Aside;

Adrenaline synthesis

Bad

Bile acid formation

Days

Degradation of tyrosine

Became

Bone mineral metabolism

Past

Potent anti oxidant

 

Iron Deficiency - Causes

Derby

A. Deficient intake

In

B. Improper utilisation

England

C. Excessive demand

1. Children 6 months - 2 years

2. Adolescents

3. Menstruation

4. Pregnancy and lactation

Beat

D. Blood loss

1. External haemorrhage

2. Menorrhagia

3. Gastrointestinal bleeding

i. Peptic ulcer

ii. Portal hypertension

iii. Oesophageal varices

iv. Ulcerative colitis

v. Amoebic dysentery

vi. Carcinoma of stomach, rectum

4. Urinary track bleeding

i. Haematuria

ii. Haemoglobinuria

5. Other bleeding

i. Epistaxis

ii. Haemoptysis

6. Parasitic infestations

- Ankylostomiasis

India

E. Iron loss without bleeding

- Exfoliative dermatitis


 

Chapter 09 : Mineral metabolism

 

Importance of Zinc in Enzyme activity

Care

1.    Carbonic anhydrase

An

2.    Alkaline phosphatase

Aged

3.    Alchol dehydrogenase

Person

4.    Porphobilinogn synthase

Living

5.    Leucine aminopeptidase

Close

6.      Carboxy peptidase

 

Deficiency of selenium

Little

1.      Liver cirrhosis

Pay

2.      Pancreatic degeneration

More

3.      Myopathy, infertility

Fame

4.      Failure of growth

 

Sugar derivatives of biomedical importance

D

 

1. Deoxy sugars

A

 

2. Amino sugars (hexosamines)

A

 

3. Amino Sugar Acids

 

 

 

Neuraminic acid

 

 

 

Muramic acid

G [Daag - Spot]

 

4. Glycosides

 

Computer

 

Cardiac glycosides

 

Operator

 

Ouabain

 

Paying

 

Phloridzin

 

Attention

 

Antibiotics – Streptomycin


 

 


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