myoglobin and haemoglobin Flashcards

1
Q

describe the components of blood

A
  • non-cellular / cellular components
  • plasma: 55%, liquid, matrix in which BC and other components are suspended (proteins, ions, metabolites, wastes, hormones), albumins (protein, bind substances, majority, osmotic pressure), globulins (antibodies, buffer), fibrinogen (clotting, produce fibres)
  • platlets: fragments of bone marrow
  • WBC: immunity
  • RBC: 45% haemoglobin, biconcave, lack nucleus
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2
Q

what is the circulatory system

A
  • closed system
  • circulates in vessels from and back to a pump (heart)
  • transportation (respiratory, nutritive, excretory)
  • regulation (hormone transpot, temperature)
  • protection (blood clotting, immune defence)
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3
Q

what is the respiratory system

A
  • ventilation, air brought to alveoli through system of branches
  • site of gas exchange = alveoli
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4
Q

how do we get oxygen from air to cells

A
  • hypothetical: oxygen delivered in solution in blood, 2L of oxygen per min from lungs to tissues (4.5mL of oxygen can dissolve in 1 L of blood)
  • actual: haemoglobin (respiratory pigment), binds oxygen to protein (not dissolved, 1.25L of oxygen per min
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5
Q

what is haemoglobin and what does it transport

A
  • 4 peptide chains
  • organic heme group (cofactor)
  • iron at centre of each heme group
  • O2 binds to each irons (4x), binding to 1st spot causes conformational shift to next group, oxygen bind with more affinity, cooperativity / alesteric interaction
  • when O2 binds CO2 is released (haldane effect)
  • oxyhaemoglobin / deoxyhaemoglobin
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6
Q

what is the oxygen dissociation curve

A
  • relationship between partial pressure of oxygen and saturation of haemoglobin
  • sigmoidal curve (characteristic binding)
  • pattern of oxygen loading / unloading
  • plateau: increasing PO2 = small yield in terms of saturation, diminishing marginal utility, saturation = 90-100%, no free sites (lungs)
  • steep curve: haemoglobin affinity for O2 increases as successive molecules bind (tissues - unloading of O2)
  • P50: half way saturation, conventional measure
  • shift: curve is not stationary shifts left to right dependent on where it is in the body
  • left shift: more affinity, high pH, low temp, low partial pressure of CO2 (foetus)
  • right shift: low pH, high temp, high partial pressure of CO2 (exercise)
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7
Q

how is carbon dioxide transported

A
  • produced by metabolism / cellular respiration
  • move through blood as 7% plasma, 23% bound to haemoglobin and 70% transported as HCO3-
  • HCO3- = CO2 diffuses into RBC, dissociates into bicarbonate, this diffuses from cell to plasma and reverse occurs there
  • CO2 + H2O - H2CO3 - HCO3- + H+
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8
Q

describe the importance of blood proteins

A

hypoproteinemia:
- deficiency of plasma protein (arms and legs are emaciated, skin is tight from edema)
- water leaving body into abdomen, not enough protein in diet, lose muscle, lack of albumin (no osmotic pressure balance), dilute blood (high water, moves into tissues)

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9
Q

what is myoglobin

A
  • secondary respiratory pigment
  • protein-iron pigment (muscle cells), like haemoglobin, reversibly binds with O2
  • temporarily stores O2 and reduces need for continuous blood supply during contraction
  • important as blood flow may decrease during muscle contraction
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10
Q

what are slow and fast twitch fibres

A
  • slow: red, long contractions without fatigue, lots of myoglobin and mitochondria (high respiratory capacity), rapidly generate ATP
  • fast: white, more susceptible to fatigue, poor blood supply, fewer myoglobin / mitochondria
  • eye muscles: white (contract 10x faster) than red (maintain posture)
  • athletes: endurance have more slow twitch, change in fibre types
  • mixture: most muscles are a mix, nurture (proportion of fibre can change) vs nature (proportion initially genetically programmed)
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