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Biochem Ca1 Cram > Proteins > Flashcards

Proteins Flashcards

1
Q

What are proteins ?

A

macromolecular polypeptides.
• Makes up the muscles, tendons, organs, glands, enzymes, some hormones, blood proteins, immunoglobulin, bones, nails and hair.
• Needed for growth, repair and maintenance of cells
• Next to water, protein makes up the greatest portion of our body weight

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2
Q

10 functions of proteins and examples

A

1.Transport ( Hb and transferrin )
2. Mobility ( actin and myosin )
3. CNS ( laminitis , nerve growth factors )
4. Wound healing regeneration , energy and satiation
5. Fluid balance ( blood proteins )
6. Acid-base regulation ( Hb, albumin )
7.Hormones (insulin , growth hormones )
8. Enzymes (amylases and pepsin)
9. Immunity ( lysozyme, antibodies)
10. Structure ( collagen, keratin, elastin)

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3
Q

8 protein classifications based on function

A
  1. Structural
  2. Enzymes
  3. Hormones
  4. Respiratory
  5. Transport
  6. Contract.
  7. Storage
  8. Toxins
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4
Q

What are amino acids

A

• Chemical units or “building blocks” of proteins

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5
Q

What are “Essential Amino Acids”

A

• A.A that must be obtained from the diet

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6
Q

What are “Nonessential Amino Acids.”

A

• A.A that the body can synthesize from other sources than diet

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7
Q

3 applications of a.a

A

• Clinical Application -Slower, Longer-Acting Insulin Created by substituting Amino Acids in the year 2000
• Heavy metal poisoning: Sulphur group in cysteine binds heavy
metals
• Electrophoresis to identify different diseases: e.g. Crohn’s disease
(decreased serine and increased histidine), Sickle cell anaemia

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8
Q

9 essential a.a

A

1.Histidine
2.leucine
3. Isoleucine
4. Lysine
5. Methionine
6. Threonine
7.Phenylalanine
8. Valine
9. Tryptophan

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9
Q

6 conditionally non-essential

A
  1. Arginine (essential mainly in children )
  2. Cystine
  3. Glutamine
  4. Glycine
  5. Proline
  6. Tyrosine
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10
Q

5 non-essential a.a

A

Alanine
Asparagine
Aspartate
Glutamate
Serine

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11
Q

What are conditional a.a

A

Body cannot synthesize some a.a in sufficient quantities during certain stages/conditions. Hence they become conditionally essential.
e.g pregnancy, adolescent growth, or recovery from trauma

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12
Q

Structure of a.a

A

Each a.a has
• a carboxyl group
• a primary amino group (proline 2ry )
• & a distinctive side chain “R group”

• At physiological pH the carboxyl group is negatively charged (COO-) & the amino group (NH3+) is protonated

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13
Q

pH of anion and cation

A

Cation is low pH
Anion is high pH

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14
Q

Properties of a.a

A

• The α-carbon of a.a is a chiral carbon
(attached to 4 different groups-asymmetric centre)
• Optically active carbon atom except Glycine.
• They have the mirror image form: D & L isomerism
Known as enantiomers

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15
Q

D and L isomers and where are they formed

A

If Amino group is present on the right side of the asymmetric (a-carbon ) is known as D isomer

• All amino acid found in protein are of L-configuration.
• D-amino acids are found in some antibiotics and in
bacterial cell walls
(drug absorption and Handerson -Hasselbalch equation)

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16
Q

Classification 7 of amino acids present in proteins

A
  1. With Aliphatic Side Chains
  2. With Side Chains Containing Hydroxylic (OH) Groups
  3. With Side Chains Containing Basic Groups
  4. Containing Aromatic Rings
  5. With Side Chains Containing Sulfur Atoms
  6. With Side Chains Containing Acidic Groups /Their Amides
  7. Imino Acid
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17
Q

Abbreviation & symbols of a.a

A

• Each a.a has a 3 letter abbreviation and one-letter codes

Glycine Gly G Threonine Thr T

Alanine Ala A Cysteine Cys C

Valine Val V Tyrosine Tyr Y

Leucine Leu L Asparagine Asn N

Isoleucine Ile I Glutamine Gln Q

Methionine Met M Aspartic Acid Asp D

Proline. Pro P Glutamic Acid Glu E

Phenyl Aline Phe F Lysine Lys K

Tryptophan. Trp W Arginine Arg R

Serine. Ser S Histidine His H

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18
Q

What is proline

A

a secondary amine, but used in the biosynthesis of proteins - Proteinogenic (20 +1 amino acid )

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19
Q

When can amino acid side chains with hydroxyl group be phosphorylated

A

During post translational modification

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20
Q

What is Isoelectric point (pl)

A

the pH at which a particular molecule or surface carries no net electrical charge .

• The net charge is affected by pH of the environment & can become more (+)vely or (-)vely charged due to loss or gain of protons (H+).

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21
Q

4 applications of pl

A

• Separation of protein
• Solubilizing protein
• Isoelectric focusing
• Predict R group

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22
Q

Correlation between charge and pl

A

At a pH below their pI, proteins carry a net positive charge; above their pI they carry a net negative charge.

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23
Q

What is isoelectric focusing

A

• Proteins can be separated according to their isoelectric point using a technique called isoelectric focusing.
• To predict R group

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24
Q

How to calc pl for a.a with only one NH2 and one COOH group

A

the pI can be calculated from the pKa’s of this molecule.

Two pKa’s used are those of the two groups that lose and gain a charge from the neutral form of the amino acid.

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25
Q

How can 2 a.a be joined

A

covalently in a condensation reaction

These are amide linkages between the α-carboxyl group of one a.a and the α-amino group of the other.

• Side chain determines the property of protein

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26
Q

5 features of peptide bond

A

Peptide bonds are not broken in normal denaturing conditions.
– has a partial double bond character: (Shorter than a single bond )
–Is rigid (between C1 and N is always closer to 180 ) and planar (due to the delocalization of the electrons from the double bond)
–Exist in trans configuration
–Is uncharged but polar
prevents free rotation around the bond :between the carbonyl carbon and the nitrogen of the peptide bond. • Peptide bond is uncharged- neither accepts nor release protons. Generally peptide bond is not available for chemical reaction except for hydrogen bond formation. Polarity depends on the N-terminal amino group, C- terminal carboxy group and any ionized chains present in the side chain.

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27
Q

How peptide bonds named

A

• Free N terminal is written to the left • Free Carboxyl terminal to the right
• A.a are read from the N to C terminal
• A.a residue having the suffix “ine, an, ic, ate” are changed to “yl” except the c-terminal

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28
Q

Hw to determine amino acid comp of polypeptide

A

peptide bonds are cleaved and a.a are released , a.a is separated by cation-exchange chromatography.

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29
Q

Ninhydrin test

A

Positive tesr is purple coloured complex

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30
Q

Sequencing of the peptide from its N-terminal end

A

• Edman Degradation

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31
Q

How determine primary structure of protein by DNA sequencing

A

• If the nucleotide sequence is determined, from the genetic code it is possible, to translate the sequence of nucleotides into the corresponding a.a of that polypeptide.

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32
Q

Structure Organization of Proteins

A

• Mainly four organizational level
• Primary, Secondary, Tertiary, Quaternary.
• The complexity increases
• Ranges from simple proteins to multifunctional proteins

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33
Q

Primary structure (Iry)

A

• Sequence of a.a in a protein (joined by peptide bonds)
• Includes the location of disulfide bond
• Deviation and abnormality in the a.a sequence may result in improper folding and loss of normal function

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34
Q

Secondary structure

A

• The conformation of the polypeptide backbones of proteins
• Commonly they form a regular arrangements with a.a close to each other : arrangements are due to the partial double bond character of the peptide bond
• 2ndry structure includes α-helix, β-sheet and β-bend
• Hydrogen bonds and Vander Waals force stabilize the 2ndry structure mainly the α-helix

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35
Q

What is a helix

A

• A common motif in the IIry structure of proteins
• The α-helix is a right- or left-handed coiled conformation
• Resembles a spring, in which every backbone N-H group donates a H bond to the backbone C=O group of the a.a four residues earlier
( hydrogen bonding).

• Spiral structure
• Tightly packed, coiled polypeptide backbone core.
Side chain extend outwards
Stabilized by H bonding b/w
carbonyl oxygen and amide hydrogen.
Amino acids per turn - 3.6
Pitch is 5.4 A
Alpha helical segments are found in many globular proteins like
myoglobins, troponin- C etc.

• It has the lowest energy and is the most stable form (stability increases with hydrogen bond formation)
• Some a.a disturb the helix
• proline may insert a kink,
• charged a.a form ionic bond and disturb the arrangement
• bulk side chain a.a may also interfere

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36
Q

Describe Beta sheet (β-sheet)

A

Unlike the alpha helix β-chain are composed of two or more peptide chains (strands) or segments of peptide chain
• All the peptide bond component are involved in hydrogen bonding
• The hydrogen bond is perpendicular
• Hydrogen bonds may be inter or intra chain bonds
• They may be parallel (C–terminals on the same side or antiparallel (C-terminals on the opposite side) or mixed (both )

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37
Q

Describe b bends / reverse turns

A

Predominant protein type in globular proteins
• Compact structure
• Predominantly found in cytosol & surface of protein molecule
• Connect strands of anti-parallel β-sheets
• Contain mainly proline (kink), glycine (smallest a.a)

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38
Q

• Non repetitive secondary structure

A

• Some polypeptides may have a loop or coil and have less regular structure
(“random coil”)

Secondary structure

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39
Q

• Super secondary structure

A

• Combines all IIry structure & assembles together
• Side chains of adjacent IIry structure elements assemble close to each other & folds into a protein

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40
Q

Describe tertiary structure

A

• IIIry structure is considered to be largely determined by the protein’s Iry or the sequence of a.a of which it is composed of
• In globular proteins , IIIry interactions are frequently stabilized
by the sequestration of hydrophobic a.a residues in the
protein core, from which water is excluded, & by the
consequent enrichment of charged or hydrophilic residues on the protein’s water-exposed surface.

41
Q

Bonds stabilizing tertiary structure

A

four types of bonding interactions between “side chains” including: hydrogen bonding, salt bridges, disulfide bonds, and non- polar hydrophobic interactions.

42
Q

What are Disulphide bonds

A

• Disulfide bonds are formed by oxidation of the sulfhydryl groups on cysteine.
• Two disulphide-linked cysteines are referred to as cystine
• Protein chains or loops within a single chain are held
together by the strong covalent disulphide bonds. e.g. albumin

43
Q

Describe Hydrogen Bonding

A

• Hydrogen bonding between “side chains” occurs in a variety of circumstances.
• The most usual cases are between two alcohols, an alcohol and an acid, two acids, or an alcohol and an amine or amide.

44
Q

Salt bridges

A

Salt bridges
• Result from the neutralization of an acid and amine on side chains.
• The final interaction is ionic between the positive ammonium group and the negative acid group.

45
Q

Non-Polar Hydrophobic Interactions

A

hydrophobic interactions of non-polar side chains are believed to contribute significantly to the stabilization of the IIIry structures
• Non-polar groups mutually repel water & other polar groups & results in a net attraction of the non-polar groups for each other.
e.g. Ala, Val, Leu, and Ile interact in this way.
• Benzene (aromatic) rings on Phe &Tyr can “stack” together.

46
Q

Quaternary (IVry)

A

• Arrangement of protein with two or more polypeptide chain (subunits)
– 2subunit-dimeric – 3subunit-trimeric
• These sub units are held together by non-covalent interactions (H- bond, ionic bonds, hydrophobic interaction)

47
Q

Write “true” or “false”.
a. Proteins are synthesised from L-amino acids.
b. Non-essential amino acids are not required for protein synthesis. c. Proline and hydroxyproline are aliphatic amino acids.
d. All amino acids can form Zwitterions.
e. Arginine is an essential amino acid in growing childre

A

TFFTT

48
Q

3 types of proteins

A

Simple — globular and scleroproteins ( fibrous proteins )
Conjugated
Derived — primary & secondary

49
Q

7 globular proteins

A

Albumins
Globulins
Prolamins
Glutelins
Histones
Protamins
Globins

50
Q

3 scleroproteins

A

Collagen
Elastins
Keratins

51
Q

6 conjugated proteins

A

Nucleoproteins
Chromoproteins
Glycoprotein
Phosphoprotein
Lipoprotein
Metalloprotein

52
Q

3 primary proteins

A

Proteans
Metaproteins
Coagulated proteins

53
Q

5 secondary proteins

A

Proteoses
Peptones
Polypeptides
Simple peptides
Amino acids

54
Q

Fibrous Vs Globular

A

Shape. Axial ratio greater > 10 Axial ratio less than 10 _ . Long & narrow Round/spherical

Solubility. Insol. Sol

Purpose. Structural. Functional

Example Collagen, myosin, Enzymes, Hb, insulin,
fibrin, Actin,a-Keratin, Immunoglobulin
elastin

Durability Less sensitive to changes More sensitive
In pH, temp etc

55
Q

What is collagen

A

• Most abundant protein in human
• Rigid insoluble protein
• In some tissue it is dispersed in the form of gel
e.g. extracellular matrix / the vitreous humour
• In some other tissues found as tight parallel fibres:
e.g. tendon
• Collagen may be stacked : e.g. cornea

56
Q

Overview of biosynthesis of collagen

A

• Formed in fibroblast or in the osteoblast of bones & chondrocytes
• Secreted into the extracellular matrix after enzymatic modification • Monomers aggregates & cross links to form collagen fibrils

57
Q

8 steps in collagen biosynthesis

A

• Genes to transcription to Translation to protein
• Formation of Pro α-chains
• Hydroxylation
• Glycosylation
• Assembly & secretion of procollagen
• Extracellular cleavage of procollagen
• Formation of collagen fibrils
• Cross link formation

58
Q

Explain hydroxylation ( post translational modification )

A

• In the RER selective hydroxylation of proline & lysine takes
place at the Y location from glycine Gly-X-Y
• Hydroxylation enzymes (prolylhydroxylase & lysyl
hydroxylase) requires molecular oxygen and vitamin C
• Hydroxyl lysine & hydroxyl proline enhances the cross
linking & strengthen the collagen

59
Q

Explain glycosylation ( post translational modification )

A

•Hydroxyl lysine can be further modified with
glucose or glucosyl – galactose

60
Q

Collagen cross links

A

Lysyl oxidase oxidatively deaminates some lysyl & hydroxylysyl residues giving rise to aldehyde groups (allysine, hydroxyallysine)

3 pro-α-chains assemble - is initiated by the disulfide cross linking of the C-terminus
helical structure in the middle & non-helical structure at the C & N terminal

Collagen molecule to microfibrils ( quarter staggered arrangement ) to fibrils

• This cross links with neighbour lysyl, & hydroxyl residues & forms covalent cross links providing tensile strength
Note:
1. Any interference to the cross linking affects the
stability of the collagen
2. Deficiency of the above processes may lead to scurvy

61
Q

What is tropocollagen and its structures

A

• The tropocollagen or “collagen molecule” is a subunit of larger collagen aggregates such as fibrils.
• Approximately 300 nm long and 1.5 nm in diameter, made up of three polypeptide strands (called alpha chains), each possessing the conformation of a left- handed helix

These three left-handed helices are twisted together into a right- handed coil, a triple helix or “super helix”, the quaternary structure are stabilized by numerous H-bonds.

62
Q

Dif in diameter of proteins

A

Amino acids approx. 1 nm
Tropocollagen approx. 300 nm
Fibrils approx. 1 um
Fibres approx. 10 um

63
Q

types of collagen

A

Fibril forming
• Type I : This is the most common collagen type found in skin,
bone, tendon, blood vessel, cornea

Type II Cartilage, intervertebral disk, vitreous body

Type III Blood vessels, fetal

     Network forming  Type IV Basement membrane

Type VII beneath stratified squamous epithelia

   Fibril-associated Type IX  cartilage

Type XII tendon, ligaments, some other tissues

64
Q

2 diseases of collagen

A

Ehlers-Danlos Syndrome ( circus man syndrome )
Osteogenesis imperfecta (brittle bone disease)

65
Q

What is elastin

A

Contrast to collagen elastin is stretchable and rubber like

• Insoluble protein synthesized from a precursor, tropoelastin (soluble polypeptide)
• Composed of small nonpolar a.a such as glycine, alanine & valine
• Even though it is rich in proline and lysine contains only little
hydroxylated a.a

66
Q

Where is elastin found

A

–Found in lungs, elastic ligaments, wall of large arteries

67
Q

Desmosine cross links of elastin

A

• Elastin fibres are formed as a 3D network of cross linked polypeptides with an irregular conformation
• Four lysine side chains from 4 different elastin molecules covalently join to produce desmosine cross links

Extensively interconnected rubbery network-to- stretch and bend

68
Q

What is α-1 Antitrypsin

A

• This enzyme inhibits number of proteolytic enzymes that hydrolyse & destroy protein- produced in liver
• Inhibits mainly trypsin
• It also inhibits neutrophil elastase which degrades
elastin in the alveoli

69
Q

Explain mutation of a1-Antitrypsin

A

• one single purine base mutation (GAG to AAG - lys for glu)
• mutation causes the normally monomeric α -AT to misfold, polymerize, and aggregate within the RER of hepatocytes
• This causes a decrease in the secretion of α -AT by the liver.
• Consequently, blood levels of AAT are reduced, decreasing the
amount that gets to the lung.

70
Q

Consequences of a-1-Antitrypsin

A

• The polymer that accumulates in the liver may result in cirrhosis

• Lung tissue cannot regenerate
• Though lung is exposed to low level of neutrophil
elastase its activity is inhibited by α-1 antitrypsin
• In deficiency of α-1 Antitrypsin Emphysema may result

smokers with α-AT deficiency are at more risk than non smokers to develop emphysema
Tx: Administration of α-1 AT and inhibitors of neutrophil elastase

71
Q

What is a-keratin

A

•They are tough fibres found in hair, nails & outer epidermal layer of mammals
•Each poly peptide has an α-helical structure
•They are rich in cysteine and form disulphide
bonds
Has weak and strong links

72
Q

What is denaturation

A

• Denaturation is the process where protein loses its native secondary, tertiary and /or quaternary structure
Note:
Iry structure is not necessarily broken in denaturation

73
Q

Desaturation agents

A

pH
Temp
Ionic strength
Solubility

74
Q

Thalassaemia

A

inherited blood disorder associated with Hb

75
Q

HbE

A

abnormal form of hemoglobin that may cause mild
anaemia

76
Q

3 characteristics of globular proteins

A

• have spheroidal shape
• have variable molecular weights,
• In water highly soluble

77
Q

3 functional roles of globular proteins

A

catalysts, transporters & regulators of metabolic pathways & gene expression.

78
Q

What is Haem

A

• Is an example of a prosthetic group, (a non-protein group tightly associated with the protein).
• It sits in a hydrophobic pocket of haemoglobin having 2 histidine one on either side of the haem.
• Consists of Fe2+ in a ring, known as a porphyrin.
• Fe2+ which is the site of oxygen binding, coordinates with the four nitrogen in the center of the ring, which all lie in one plane.

• iron is also bound strongly to the globular protein via the imidazole ring of the histidine residue below the porphyrin ring.
• A sixth position can reversibly bind oxygen by a covalent bond, completing the six ligands.
• When oxygen is not bound, a very weakly bonded water molecule fills the site.

79
Q

Iron in Fe3+ state binding yo o2

A

• The iron in the Fe3+ state (Methaemoglobin) cannot bind oxygen.
• Binding, oxygen temporarily oxidizes Fe2+ to Fe3+.
• The enzyme Methaemoglobin reductase reactivates to Fe2+

80
Q

What is myoglobin

A

• Present in heart and skeletal muscle.

• Single chain globular protein of 153 amino acids

• It gives muscle tissue a distinct red or dark gray colour.

81
Q

Function of Mb

A

• Functions both as a reservoir for oxygen, and as an oxygen carrier that increases the rate of transport of oxygen within the muscle cell.

82
Q

Structure of Mb

A

• Mb is similar to Hb in structure and sequence but it is a monomer (Compare the tetramer structure of Hb) hence lacks cooperative binding.
• Globin (α-helical protein) consists of a single polypeptide chain (structurally similar to the individual subunit polypeptide chains of Hb)
• Polypeptide chain is folded into eight stretches of α-helix which is disturbed by proline.

• Interior of the myoglobin molecule is composed almost entirely of nonpolar a.a (binds the haem group by non covalent bond) except two histidine residues.
• one, binds directly to the iron of haem and the other helps stabilize the binding of O2to Fe2+
• charged amino acids are located almost exclusively on the surface of the molecule,

83
Q

What is uniqueness of Mb

A

• Myoglobin is an unusual protein as it comprises exclusively (80%) of α-helices joined by short loops.
• Most proteins have both α-helices and β-sheets.

84
Q

Mb Vs Hb

A

-Higher O2 affinity. - cooperative binding = sigmoidal curve
-Responds to muscle’s. - responds to O2 availability
O2 needs
- curve that flattens - O2 binding properties of Hb regulated
- 1 Haem group so 1 O2. By interaction with allosteric effectors

                                               - can transport H+ and CO2
85
Q

What is Hb

A

• Is an iron containing oxygen transport metalloprotein in the RBC.
.

86
Q

4 roles of Hb

A

• Function is to transport
1.oxygen from the lungs to the capillaries of the tissues.
2.CO2 from the capillaries of the tissues to lungs.
3.NO: e.g S-nitrosohemoglobin (SNO-Hb), which can deliver the
NO to areas of hypoxia or restricted blood flow
I4.mportant role as an efficient buffer (pH of histidine side
chain)

87
Q

Structure of haemoglobin

A

• Haemoglobin A, the major hemoglobin in adults, is composed of four polypeptide chains—2 α chains and 2 β chains—held together by noncovalent interactions
• Each subunit has stretches of α-helical structure, and a haem-binding pocket similar to that of Mb.

88
Q

Quaternary structure of Hb

A

• The haemoglobin tetramer can be envisioned as being composed of two identical dimers, (α1β1)and (α2β2) in which the numbers refer to dimers one and two.
• The two polypeptide chains within each dimer are held tightly together, primarily by hydrophobic interactions

In this instance, hydrophobic amino acid residues are localized not only in the interior of the molecule, but also in a region on the surface of each subunit.
• Inter chain hydrophobic interactions form strong associations between α-subunits and β-subunits

• Ionic and hydrogen bonds are also present
• The two dimers are able to move with respect to each
other, being held together primarily by polar bonds.
• The weaker interactions between these mobile dimers result in the two dimers occupying different relative positions in deoxyhaemoglobin as compared with oxyhaemoglobin

89
Q

4 main Bonds stabilizing the Hb molecules (4 polypeptide chains)

A

• Salt bridges (ionic bond)
• Hydrogen bond
• Hdrophobic interactions

90
Q

2 kinds of contacts between a & B chains

A

Taut (T-tensed)
Relaxed (R) form

91
Q

What is T form: (low-oxygen-affinity )

A

Deoxy form of haemoglobin
• The two αβ dimers interact through a network of ionic bonds and hydrogen bonds that constrain the movement of the polypeptide chains.

Some of these bonds broken in oxygenated state

92
Q

R form (high oxygen affinity)

A

• Binding of oxygen to Hb causes the rupture of some of the ionic bonds and hydrogen bonds between the αβ dimers.
• Here the polypeptide chains have more freedom of movement

93
Q

Explain Synthesis of Haemoglobin

A

• Is synthesized in a complex series of steps.
• The haem part is synthesized in the mitochondria
and cytosol of immature red blood cells
• The globin protein parts are synthesized by
ribosomes in the cytosol

94
Q

Binding of other gases ( CO2)

A

Most of CO2 produced in metabolism is hydrated and transported as bicarbonate ion

• Some CO2 is carried as carbamate bound to the uncharged α-amino groups of hemoglobin
• CO2 is more readily dissolved in deoxygenated blood,

• Binding of CO2 stabilizes the R resulting in a decrease in its affinity for oxygen.
• In the lungs, CO2 dissociates from the haemoglobin, and is released in the breath.

95
Q

Oxy vs deoxy Hb

A

• Oxyhaemoglobin is formed during respiration when oxygen binds to the haem component of the protein Hb in RBC.
• Deoxyhaemoglobin is the form of haemoglobin without the bound oxygen.

96
Q

What is carboxy Hb

A

• CO binds tightly to haemoglobin
• Bind to one/four of the haem sites
• Oxygen dissociation curve becomes hyperbolic (left shift)
• Unable to release oxygen to the tissues
• Affinity of haemoglobin for CO is 200-300 times greater than that of oxygen

97
Q

True /False
I. Proline residues play an important role in the formation of α – helix.
II. Quaternary structure is essential for the functioning of every protein.
III. All proteins are coagulated when they are heated at their isoelectric pH.
IV. Collagen is a right-handed triple helix.
V. Abnormal collagen is formed in Ehlers-Danlos syndrome.

A

FFTTT

98
Q

5 Indication for Hb estimation

A

• Determining the presence and severity of anaemia • Screening polyycythaemia
• Estimation of red cell indices
• Selection of blood donors
• Response to specific therapy in anaemia

Biochem Ca1 Cram (13 decks)

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