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19 Cards in this Set
- Front
- Back
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Heme needs to be in what state to function correctly?
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+2
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Glutathiones function?
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prevents oxidation of important things such as heme - it is good character for job because has cysteine, so has sulfhydrol group that can be oxidized to form disulfide bridge (which can be broken/reduced)
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How is glutathione reduced after taking hit for heme and other agents?
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NADPH-->NADP is nucleotide from pentose phosphate pway (reduced NAD+-->NADPH)
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Methemoglobin reductase functions?
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a secondary process to glutathione to rereduce iron to +2 (from +3)
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Starting materials for heme synthesis?
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succinyl CoA, glycine, heme +2
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Heme synthesis occurs where?
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reticulocytes (immature RBCs), hepatocytes in spleen, etc
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Aminolevunlinic acid (ALA) synthase?
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regulated enzyme requires B6 cofactor & feedback inhibited by heme
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Lead ... does what to heme synthesis?
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Just know that it generally inhibits synth, anemia may result & problems w energy production may occur (cytochromes for oxidative phosphor)
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Porphyrias ...?
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block synthesis bc defective enzymes, building up intermediates...body tries to move to places out of way--> neuro area causing
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Transferrin
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transports heme in blood
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Ferritin
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assists in gut absorption & short term storage
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Hemosiderin
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long term storage heme (most iron storage occurs in liver)
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Who is responsible for transport in blood to liver for conjugation?
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albumin
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Bilirubin diglucuronide
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produced via hepatic conjugation of bilirubin
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Glucuronyl transferase
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catalyzes conjugation of biliwubin
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UDP-substrate
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provides energy for conjugation from UTP/UDP blah blah
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Bilirubin diglucuronide is excreted where and broken down to?
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gall bladder, urobilinogen & stercobilin
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jaundice defined as/caused by
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inc serum bilirubin, conj or unconj
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Conjugated is or not albumin bound? --- directly/indirectly measured?
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Not, directly
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