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Module 2 vet med > Blood biochemistry > Flashcards

Blood biochemistry Flashcards

1
Q

Roles of the blood

A

Transports essiential nutrients to tissues- includes oxygen
Removes waste products
Protects against infection
Repair of tissue damage

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2
Q

Components of blood

A

Cells- in fluid called plasma
Erythrocytes- rbc- transports oxygen
Leukocytes- wbc- protects against infection
Platelets- thrombocytes- blood clotting

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3
Q

What are globulins

A

Oxygen carrying molecules

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4
Q

What is a blood smear good for

A

Helpful in diagnosis

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5
Q

What stain can u see a giesma stain in

A

Nucleated cells

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6
Q

Albumin has two main roles

A
  1. Transport by albumin
  2. Albumin in osmotic regulation
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7
Q

Albumin is from

A

Liver

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8
Q

What type of transporter is albumin

A

Non specific

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9
Q

Immunoglobulins features

A

Lymphocyte
Metal ion binding proteins
Hormone binding proteins
From liver

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10
Q

Transport by albumin involves

A

Fatty acids
Sterols
Hydrophobic molecules- toxic to cell membrane
Drugs- may be hydrophobic ie.penicillin

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11
Q

Bilirubin properties

A

Hydrophobic
Toxic

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12
Q

Albumin is important in what

A

Solubilisation
Transport and removal of hydrophobic molecules

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13
Q

Albumin in osmotic regulation features

A

High conc of plasma
Prevents tissues taking up excess water

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14
Q

What happens to albumin in severe malnutrition

A

Albumin broken down for amino acids and this causes osmolarity of plasma decreases as there is less protein and water enters tissue- oedema.

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15
Q

What is oedema

A

Water entering tissue

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16
Q

Where do we also see oedema

A

Kidney disease
Heavy parasitic infection

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17
Q

What does albumin transport

A

Divalent and trivalent cations

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18
Q

What does transferrin transport

A

Iron

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19
Q

What does ceruloplasmin transport

A

Copper

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20
Q

In vivo

A

Plasma and cells

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21
Q

In vitro

A

Serum and cells

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22
Q

Haemostasis

A

Arrest of bleeding

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23
Q

What do erythrocytes do

A

Transport of oxygen, carbon dioxide and hydrogen
Haemoglobin
Hb synthesised in eryhtroblask which is an early immature cell
Life span- 60-120days

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24
Q

What is spectrin

A

Peripheral protein that lies beneath the membrane and forms the cytoskeleton

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25
Q

Peripheral protein is

A

Outside

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26
Q

Integral protein is

A

Inside

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27
Q

What other peripheral proteins does spectrum interact with

A

Ankyrin
Actin
Protein 4.1

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28
Q

What is the functional protein of spectrin

A

Mechanical stability
Resilience to membrane
Helps withstand shearing forces and pressure changes while in blood circulation

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29
Q

Lipid examples

A

Phospholipids
Sphingolipids
Cholesterol
This provides mobility to the cell membrane and allow it to move

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30
Q

There is 4 important integral proteins, what are they

A

Glycoprotein A
GLUT 1
Sodium potassium pump
Anion exchanger

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31
Q

Glycoprotein A features

A

Extracellular region- rich in COOH
Transmembrane domain
Cytosolic domain
COOH rich in saline acid and is negative charge- hydrophilic
This prevents RBCs sticking to other cells and cell walls

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32
Q

What determines blood group type

A

Glycosylation of proteins and lipids on extracellular domain

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33
Q

Why is blood transfusion need to be a match

A

As the cells will destroy each other

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34
Q

What is GLUT1

A

Glucose transporter

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35
Q

What type of diffusion does GLUT1 use

A

Facilitated- glucose into RBC for glycolysis and PPP

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36
Q

What does the sodium potassium pump do

A

Maintain correct balance

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37
Q

What type of channel is a anion channel

A

Dimeric protein- exchange of carbonate ion and chloride ion

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38
Q

What is an anaerobic reaction

A

No mitochondria is present so no oxygen reaction

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39
Q

What is NADPH used for in an anaerobic reaction

A

Reducing activity generated by Penrose phosphate pathway

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40
Q

Steps of the Pentose phosphate pathway

A

NADP to NADPH- needed in rbc
Glu-6-P to pentose phosphates to nucleotides

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41
Q

Oxidation of heme is caused by

A

High oxygen and heme iron.
ROS is formed in rbcs

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42
Q

What are Heinz bodies

A

When o2 does not bind and precipitates into rbc

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43
Q

Why do rbc need NADPH

A

Rbc carries 02 which is a strong oxidising agent in presence of metal ions
O2 becomes reduced and forms a reactive oxygen species- ROS

44
Q

How are ROS produced

A

Phagocytosis

45
Q

What is a negative of ROS

A

Cause damage to cell membrane lipid and proteins

46
Q

What is the purpose of antioxidant defence?

A

To remove toxic oxygen
To remove oxidised proteins

47
Q

What are two methods of antioxidant defence

A

Glutathione
NADH/ cytochrome b5 methhaemoglobin reductase

48
Q

Why is pentose phosphate pathway needed

A

As NADPH is needed in rbc to maintain glutathione in reduced state

49
Q

What does GSH do

A

Non enzymatically reverses oxidation of proteins

50
Q

What happens to GSH when it reverses oxidation of proteins

A

It itself becomes oxidised and turns into GSSG

51
Q

Why must GSH be regenerated

A

To prevent protein denaturation

52
Q

What is methemoglobinemia

A

Defect in methemoglobin reductase

53
Q

Is methemoglobin hereditary

A

Yes

54
Q

What are examples of chemical, drug or diet induced toxins

A

Paracetamol
Onions
Garlic
Rye grass
Maple leaf

55
Q

What are clinical signs of methemoglobinemia

A

Cyanosis
Exercise intolerance
Vomiting
Chocolate brown blood
Anaemia

56
Q

What enzyme aids in the generation of carbonate

A

Carbonic anhydrase

57
Q

What type of protein pump is used in generation of carbonate

A

Anion exchanger

58
Q

What is a feature of aerobic

A

Requires oxygen

59
Q

Why does oxygen need to be transported

A

It has a low solubility

60
Q

What acts as the oxygen transporter

A

Haemoglobin

61
Q

What is the name of the oxygen store in muscles

A

Myoglobin

62
Q

What is a prosthetic group

A

Haem group

63
Q

What are the organic components of heme

A

Carbon
Nitrogen
Oxygen
Hydrogen

64
Q

Iron is bonded to what number of nitrogens

A

4

65
Q

What places are the additional binding sites at

A

5 and 6

66
Q

What is a distal histidine

A

Important for reducing carbon dioxide binding

67
Q

Is carbon monoxide poisonous

A

Yes

68
Q

What has higher affinity to Haemoglobin and myoglobin

A

Carbon monoxide

69
Q

What decreases Haemoglobin affinity for carbon monoxide

A

Distal histidine

70
Q

Haem function is modulated by

A

Protein environment

71
Q

What does allosteric mean

A

Other shape

72
Q

What happens when small molecules and oxygen are bound

A

The protein changes shape and ligand affinity

73
Q

Allosteric allows how many subunits to bind

A

4

74
Q

What does allosteric binding do

A

Binding at 1 site affects shape/ affinity of other sites

75
Q

Is myoglobin allosteric

A

No it only has one binding site

76
Q

What structure is Haemoglobin

A

Quarternary

77
Q

Deoxyribose features

A

Lower oxygen affinity
Tense
Extra ionic bonds
Also ionic bonds with 2,3 BPG

78
Q

Oxyribose feature

A

Higher oxygen affinity
Relaxed- r form
Rotation at contact

79
Q

Myoglobin features

A

1 polypeptide chain
1 heme group
1 O2 binding site per molecule

80
Q

Haemoglobin feature

A

4 polypeptide chain
4 heme group
4 O2 binding sites per molecule
Allosteric protein

81
Q

What are allosteric effectors

A

CO2
H
2-3 BiPglycerate

82
Q

What do negative effectors do

A

Bind to Hb at different site to O2

83
Q

Oxygen dissociation curve

A

Myoglobin strict increase
Haemoglobin steady increase

84
Q

What are the effects of 2,3 BPG

A

Moves curve to the right

85
Q

O2 deprivation causes

A

An increase in 2,3 BPG
Stablises deoxy Hb which promotes release of 02 in tissues

86
Q

What can be the causes of 2,3 BPG

A

Anaemia
Cardiac failure
High altitude

87
Q

What kind of curve does myoglobin have

A

Hyperbolic
No interaction between binding sites

88
Q

What kind of curve does Haemoglobin have

A

Sygmodial
There is interaction between binding sites
Low 02 affinity

89
Q

Heme removal pathway

A

Heme to biliverdin to bilirubin to bile to metabolised in gut and then excreted in faeces

90
Q

What does EPO increase

A

Red blood cell production

91
Q

What can cause rbc production

A

High altitude
Hypoxia

92
Q

What is EPO

A

Erythropoietin

93
Q

What causes an enhanced performance

A

EPO from kidney

94
Q

What is sickle cell animal

A

Genetic defect in B globulin gene

95
Q

What is HbS

A

Sickle cell haemoglobin

96
Q

What does deoxyHb do in sickle cell disease

A

Forms polymers and precipitates inside rbcs which changes shape

97
Q

What is another symptom in sickle cell

A

Lysis as they can become trapped

98
Q

Symptoms of sickle cell anaemia

A

Exercise intolerance
Cramps

99
Q

Why in Africa is sickle cell anaemia a form of positive selection

A

Gives protection against malaria

100
Q

What is the lifespan of rbcs

A

60-120

101
Q

Where are rbcs degraded

A

The spleen

102
Q

Where is heme synthesised

A

Liver and early rbcs

103
Q

Synthesis defects

A

Porphyria compound in cells
Red discolouration of teeth and bones
Photodermatitis
Anaemia

104
Q

Why do holstein calves protect from the sun

A

Sensitive to UV light

105
Q

What is jaundice

A

When there is elevated bilirubin levels in plasma

106
Q

What does jaundice cause

A

Yellow colour in skin
Yellow mucous membrane
Decrease in albumin binding
Impaired liver function

Module 2 vet med (16 decks)

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