Blood biochemistry Flashcards by Mirren Stride

Roles of the blood

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

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Components of blood

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

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What are globulins

Oxygen carrying molecules

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What is a blood smear good for

Helpful in diagnosis

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What stain can u see a giesma stain in

Nucleated cells

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Albumin has two main roles

Transport by albumin
Albumin in osmotic regulation

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Albumin is from

Liver

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What type of transporter is albumin

Non specific

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Immunoglobulins features

Lymphocyte
Metal ion binding proteins
Hormone binding proteins
From liver

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Transport by albumin involves

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

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Bilirubin properties

Hydrophobic
Toxic

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Albumin is important in what

Solubilisation
Transport and removal of hydrophobic molecules

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Albumin in osmotic regulation features

High conc of plasma
Prevents tissues taking up excess water

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What happens to albumin in severe malnutrition

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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What is oedema

Water entering tissue

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Where do we also see oedema

Kidney disease
Heavy parasitic infection

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What does albumin transport

Divalent and trivalent cations

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What does transferrin transport

Iron

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What does ceruloplasmin transport

Copper

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In vivo

Plasma and cells

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In vitro

Serum and cells

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Haemostasis

Arrest of bleeding

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What do erythrocytes do

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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What is spectrin

Peripheral protein that lies beneath the membrane and forms the cytoskeleton

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Peripheral protein is

Outside

Integral protein is

Inside

What other peripheral proteins does spectrum interact with

Ankyrin Actin Protein 4.1

What is the functional protein of spectrin

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

Lipid examples

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

There is 4 important integral proteins, what are they

Glycoprotein A GLUT 1 Sodium potassium pump Anion exchanger

Glycoprotein A features

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

What determines blood group type

Glycosylation of proteins and lipids on extracellular domain

Why is blood transfusion need to be a match

As the cells will destroy each other

What is GLUT1

Glucose transporter

What type of diffusion does GLUT1 use

Facilitated- glucose into RBC for glycolysis and PPP

What does the sodium potassium pump do

Maintain correct balance

What type of channel is a anion channel

Dimeric protein- exchange of carbonate ion and chloride ion

What is an anaerobic reaction

No mitochondria is present so no oxygen reaction

What is NADPH used for in an anaerobic reaction

Reducing activity generated by Penrose phosphate pathway

Steps of the Pentose phosphate pathway

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

Oxidation of heme is caused by

High oxygen and heme iron. ROS is formed in rbcs

What are Heinz bodies

When o2 does not bind and precipitates into rbc

Why do rbc need NADPH

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

How are ROS produced

Phagocytosis

What is a negative of ROS

Cause damage to cell membrane lipid and proteins

What is the purpose of antioxidant defence?

To remove toxic oxygen To remove oxidised proteins

What are two methods of antioxidant defence

Glutathione NADH/ cytochrome b5 methhaemoglobin reductase

Why is pentose phosphate pathway needed

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

What does GSH do

Non enzymatically reverses oxidation of proteins

What happens to GSH when it reverses oxidation of proteins

It itself becomes oxidised and turns into GSSG

Why must GSH be regenerated

To prevent protein denaturation

What is methemoglobinemia

Defect in methemoglobin reductase

Is methemoglobin hereditary

Yes

What are examples of chemical, drug or diet induced toxins

Paracetamol Onions Garlic Rye grass Maple leaf

What are clinical signs of methemoglobinemia

Cyanosis Exercise intolerance Vomiting Chocolate brown blood Anaemia

What enzyme aids in the generation of carbonate

Carbonic anhydrase

What type of protein pump is used in generation of carbonate

Anion exchanger

What is a feature of aerobic

Requires oxygen

Why does oxygen need to be transported

It has a low solubility

What acts as the oxygen transporter

Haemoglobin

What is the name of the oxygen store in muscles

Myoglobin

What is a prosthetic group

Haem group

What are the organic components of heme

Carbon Nitrogen Oxygen Hydrogen

Iron is bonded to what number of nitrogens

What places are the additional binding sites at

5 and 6

What is a distal histidine

Important for reducing carbon dioxide binding

Is carbon monoxide poisonous

Yes

What has higher affinity to Haemoglobin and myoglobin

Carbon monoxide

What decreases Haemoglobin affinity for carbon monoxide

Distal histidine

Haem function is modulated by

Protein environment

What does allosteric mean

Other shape

What happens when small molecules and oxygen are bound

The protein changes shape and ligand affinity

Allosteric allows how many subunits to bind

What does allosteric binding do

Binding at 1 site affects shape/ affinity of other sites

Is myoglobin allosteric

No it only has one binding site

What structure is Haemoglobin

Quarternary

Deoxyribose features

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

Oxyribose feature

Higher oxygen affinity Relaxed- r form Rotation at contact

Myoglobin features

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

Haemoglobin feature

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

What are allosteric effectors

CO2 H 2-3 BiPglycerate

What do negative effectors do

Bind to Hb at different site to O2

Oxygen dissociation curve

Myoglobin strict increase Haemoglobin steady increase

What are the effects of 2,3 BPG

Moves curve to the right

O2 deprivation causes

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

What can be the causes of 2,3 BPG

Anaemia Cardiac failure High altitude

What kind of curve does myoglobin have

Hyperbolic No interaction between binding sites

What kind of curve does Haemoglobin have

Sygmodial There is interaction between binding sites Low 02 affinity

Heme removal pathway

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

What does EPO increase

Red blood cell production

What can cause rbc production

High altitude Hypoxia

What is EPO

Erythropoietin

What causes an enhanced performance

EPO from kidney

What is sickle cell animal

Genetic defect in B globulin gene

What is HbS

Sickle cell haemoglobin

What does deoxyHb do in sickle cell disease

Forms polymers and precipitates inside rbcs which changes shape

What is another symptom in sickle cell

Lysis as they can become trapped

Symptoms of sickle cell anaemia

Exercise intolerance Cramps

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

Gives protection against malaria

What is the lifespan of rbcs

60-120

Where are rbcs degraded

The spleen

Where is heme synthesised

Liver and early rbcs

Synthesis defects

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

Why do holstein calves protect from the sun

Sensitive to UV light

What is jaundice

When there is elevated bilirubin levels in plasma

What does jaundice cause

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