1984
DOI: 10.1002/cbf.290020107
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Specific molybdenum binding to spectrin subunits

Abstract: Molybdenum in the form of its pentavalent complex binds primarily to spectrin when incubated with erythrocytes. Only the band 1 subunit is involved in this interaction thus indicating some structural differences between spectrin subunits.

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Cited by 5 publications
(1 citation statement)
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“…Once consumed, molybdenum is transported through the gastrointestinal tract via what was hypothesised to be a passive, non-mediated process, although the exact mechanism and location of the transporters remain unclear, and recent research indicates the existence of higher-affinity molybdenum transporters [27,64]. Absorbed molybdenum is rapidly detectable in blood, with a fraction reportedly binding to α2-macroglobulins, and to the cytoskeletal protein spectrin in the erythrocyte membrane, with the majority remaining unbound as molybdate [63][64][65][66]. The molybdenum cofactor, Moco, is sensitive to oxidation, so it is postulated to exist in a protein-bound state in the cell [28].…”
Section: Bioavailability and Intake Of Molybdenummentioning
confidence: 99%
“…Once consumed, molybdenum is transported through the gastrointestinal tract via what was hypothesised to be a passive, non-mediated process, although the exact mechanism and location of the transporters remain unclear, and recent research indicates the existence of higher-affinity molybdenum transporters [27,64]. Absorbed molybdenum is rapidly detectable in blood, with a fraction reportedly binding to α2-macroglobulins, and to the cytoskeletal protein spectrin in the erythrocyte membrane, with the majority remaining unbound as molybdate [63][64][65][66]. The molybdenum cofactor, Moco, is sensitive to oxidation, so it is postulated to exist in a protein-bound state in the cell [28].…”
Section: Bioavailability and Intake Of Molybdenummentioning
confidence: 99%