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Biochemistry > Blood Biochemistry > Flashcards

Blood Biochemistry Flashcards

1
Q

What is the most abundant blood protein?

A

Albumin

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2
Q

What is the purpose of blood?

A

Transports nutrients to tissues, carries waste away from tissues, protects against infection, repairs tissue damage

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3
Q

What two complexes interact with oxygen throughout the body?

A

Hemoglobin transports oxygen in RBCs, myoglobin stores oxygen in muscles

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4
Q

Which three types of cells are found in the blood (In order from most abundant to least abundant)?

A

Erythrocytes, leukocytes, platelets

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5
Q

What are the granules of granulocytes filled with?

A

Enzymes/histamines

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6
Q

What proteins are found in the plasma?

A

Albumin, immunoglobulins (Lymphocytes), some metal and hormone binding proteins

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7
Q

What are the two main roles of albumin?

A

Transport of hydrophobic molecules in hydrophilic plasma (Fatty acids, sterols, drugs, bilirubin, metals) and maintains osmotic balance between plasma/tissues (Prevents tissues from taking up too much water)

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8
Q

What happens to albumin in cases of severe malnutrition?

A

Broken down to AAs to be utilized, decreases plasma osmolarity, causes edema

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9
Q

Which metal ions will albumin circulate in the plasma?

A

Di-/trivalent ions (Fe+3, Cu+2)

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10
Q

What is the purpose of transferrin?

A

Binds Fe+3 for transport and to protect against toxicity

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11
Q

What is ceruloplasmin?

A

A protein that carries Cu+2 through the plasma

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12
Q

Which anions are found in the plasma?

A

Cl-, HCO3-, PO4-

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13
Q

Which cations are found in the plasma?

A

Na+, K+, Mg+2, Ca+2

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14
Q

Which small molecules are found in the plasma?

A

Glucose, lactate, pyruvate

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15
Q

What is the difference between serum and plasma?

A

Plasma is what is found circulating the body, fluid plus proteins. Serum is what is found after letting the blood clot (Which separates fibrinogen out of the serum).

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16
Q

How can plasma be studied outside of the body?

A

By adding an anticoagulant (EDTA, Heparin)

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17
Q

What is a zymogen?

A

An inactive precursor of an enzyme

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18
Q

Why is the blood clotting cascade tightly regulated?

A

To prevent blood clots from entering the circulation

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19
Q

What is the function of a RBC?

A

To transport CO2, O2, H+ between lungs/tissues

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20
Q

Where is hemoglobin synthesized?

A

In erythroblasts

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21
Q

What are erythroblasts?

A

Early cell found in bone marrow that still has ribosomes, mitochondria, and nucleus

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22
Q

Which lipids make up the RBC membrane?

A

Phospholipids, sphingolipids, and cholesterol

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23
Q

Which peripheral protein provides the cytoskeletal support of a RBC?

A

Spectrin

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24
Q

How do spectrin, ankyrin, and actin interact in the RBC membrane?

A

Spectrin, an internal peripheral protein, binds to actin within the membrane and ankyrin attached to an integral anion channel to provide structure yet flexibility for the RBC

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25
Q

Name four important integral proteins.

A

Glycophorin A, Glut 1 (Transports glucose into cell), Na+/K+ ATPase, and anion exchanger

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26
Q

Name several properties of Glycophorin A.

A

Contains high amounts of carbohydrate (-COOH), hydrophilic, anionic, glycosylation occurs on the outside of the protein, and negative charge prevents RBCs from sticking in circulation

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27
Q

How is blood type determined?

A

Glycosylation of proteins/lipids on extracellular domain, each specific type determined by specific glycosyl transferase

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28
Q

What does DEA stand for in terms of dog blood?

A

Dog Erythrocyte Antigen

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29
Q

Which two substances does the dimeric anion channel exchange?

A

HCO3- and Cl-

30
Q

How does CO2 contribute to the production of bicarbonate?

A

CO2 passes into RBC and reacts via carbonic anhydrase to create carbonic acid. This is then dissociated to H+ (To be used with hemoglobin) and HCO3- (To be used in the anion channel to maintain pH).

31
Q

How is CO2 excreted by the lungs?

A

Bicarbonate from plasma brought into cell via anion channel, combines with H+ from hemoglobin (Released when O2 binds to Hb) to form carbonic acid, carbonic acid dissociates to water and CO2, then CO2 passes into lungs and is breathed out

32
Q

Describe the formation of 2,3-BPG and what it does.

A

1,3-BPG transformed to 2,3-BPG by BPG isomerase, decreases affinity for O2 in RBCs so that it can be released into tissues

33
Q

Why is the PPP important in RBCs?

A

Need NADPH for reducing activity to neutralize reactive oxygen species (Which damage lipids, RBCs, and proteins)

34
Q

What happens when heme iron steals an electron from O2?

A

O2- (ROS) forms along with methemoglobin which does not bind O2 and precipitates in the RBC

35
Q

How do RBCs protect against ROS?

A

Glutathione, NADH/Cytochrome b5 methemoglobin reductase, and superoxide dismutase and catalase enzymes

36
Q

Why is NADH needed in addition to glutathione?

A

NADH keeps glutathione in a reduced state

37
Q

What does glutathione do?

A

Non-enzymatically reverses oxidation of proteins

38
Q

What does regeneration of GSH (Glutathion) from GSSG require?

A

NADH and glutathione reductase

39
Q

Between GSH and GSSH, which is reduced and which is oxidized?

A

GSH is reduced, GSSG is oxidized

40
Q

How is methemoglobinemia hereditarily caused in dogs?

A

Defect in methemoglobin reductase

41
Q

How can chemicals/diet/drugs induce methemoglobinemia?

A

Paracetamol (Aspirin) in cats, onions/garlic in dogs, rye grass/fertilizers in cattle, red maple leaf in horses, metabolism of all of these substances results in ROS

42
Q

What are the clinical signs of methemoglobinemia?

A

Cyanosis (Purple tongue/mucus membranes), exercise intolerance, vomiting, chocolate brown blood, occasionally anemia

43
Q

Where does red muscle get its color?

A

Myoglobin

44
Q

What are hemoglobin and myoglobin made of?

A

Protein and heme (Prosthetic group, the organic part of the molecule)

45
Q

What does heme contain?

A

C, H, O, N, and an iron atom

46
Q

What is the structure of hemoglobin?

A

Tetrapyrrole ring structure with iron in the middle (Hydrophobic), iron has two open binding sites left

47
Q

What is the majority of the structure of myoglobin?

A

Alpha helices in a planar orientation, also contains hydrophobic pocket with two histidines (Proximal and distal) for oxygen binding, outside has polar AAs

48
Q

On which histidine’s iron molecule does oxygen bind to to change from deoxyhemoglobin (Or deoxymyoglobin) to oxyhemoglobin (Or oxymyoglobin)?

A

Proximal histidine

49
Q

What is the purpose of the distal histidine?

A

To block O2 from binding to two heme groups via steric hindrance, forming a Fe-O-O-Fe complex (Which cannot carry oxygen), and also decreases hemoglobin’s affinity for CO

50
Q

What is another name for methemoglobin?

A

Ferrihemoglobin

51
Q

How do hemoglobin and myoglobin differ from each other?

A

Hemoglobin: 4 polypeptide chains, 4 heme groups, 4 binding sites per molecule (Allosteric molecule)

Myoglobin: 1 polypeptide chain, 1 heme group, 1 binding site per molecule

52
Q

What is HbA and what is it comprised of?

A

Adult hemoglobin, 2 alpha chains and 2 beta chains

53
Q

What is HbF and what is it comprised of?

A

Fetal hemoglobin, 2 alpha chains and 2 gamma chains

54
Q

Is myoglobin allosteric?

A

No

55
Q

How are deoxy Hb and oxy Hb different from each other?

A

Deoxyhemoglobin: Lower O2 affinity, tense (T) form, extra ionic bonds, ionic bonds with 2,3-BPG

Oxyhemoglobin: Higher O2 affinity, relaxed (R) form, rotation at contact points

56
Q

Which has a higher affinity for O2 binding: Hemoglobin or myoglobin?

A

Myoglobin

57
Q

Which effectors have a negative affect on hemoglobin?

A

CO, H+, 2,3-BPG

58
Q

How does 2,3-BPG reduce hemoglobin’s affinity for oxygen?

A

Binds to deoxyhemoglobin and stabilizes it

59
Q

How does 2,3-BPG’s effect on hemoglobin aid the body in times of oxygen deprivation?

A

Stabilizes deoxyhemoglobin and promotes release of oxygen in tissues

60
Q

How can erythropoietin (EPO) help an animal with oxygen deprivation?

A

Increases the amount of RBCs and therefore the amount of oxygen reaching the tissues

61
Q

How do sheep and goats release oxygen into the tissues in times of high CO2 levels?

A

Hemoglobin C

62
Q

How does oxyglobin aid cattle in times of oxygen deprivation?

A

Has a decreased O2 affinity which promotes O2 release into tissues

63
Q

What is the cause of Sickle Cell Anemia?

A

A defect in a beta-globin gene (HbS), the deoxygenated HbS forms polymers and precipitates inside RBCs causing a sickle shape that lyses easily and gets stuck inside vessels

64
Q

What amino acid switch is responsible for the development of Sickle Cell Anemia?

A

Glutamic Acid to Valine

65
Q

Where is heme mainly produced and by what cells?

A

Liver (Erythroblasts) and early RBCs (Reticulocytes)

66
Q

What happens when porphyrin compounds in body tissues?

A

Red/brown teeth, bones, photodermatitis (UV damage to lipids and proteins), anemia

67
Q

Why should some Holstein calves be protected from sunlight?

A

Congenital Erythropoietic Porphyria

68
Q

Where are old RBCs degenerated?

A

Spleen

69
Q

What happens to the globin and the heme in a RBC that is being degraded?

A

Globin is hydrolyzed into AAs, heme is linearized and catabolized

70
Q

What happens if a RBC lyses before it reaches the spleen?

A

Haptoglobin in plasma binds the free Hb (Which has dimerized)

71
Q

What is the sequence of heme degradation?

A

Heme (In spleen) > Biliverdin > Bilirubin > Bilirubin Diglucuranide (In liver) > Bile > Metabolized in gut > Excreted in feces

72
Q

What is jaundice and what does it cause?

A

Elevated level of bilirubin (May be due to drug decreasing bilirubin binding), causes yellowing of mucus membranes and skin, indicates an excessive breakdown of RBCs, decrease of albumin/binding, impaired liver function, or obstructed bile duct

Biochemistry (14 decks)

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