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• W2090925355 abstract "The percentage of tropomyosin and troponin in rabbit psoas muscle was estimated to be 4.2% and 5.6% of the myofibrillar protein, respectively. This suggests that on the thin filament there are two molecules of tropomyosin per 390 Å, and probably two molecules of the troponin complex. Approximately 60% of the calcium bound by troponin was accounted for by the component which conferred the calcium sensitivity, troponin A. The binding data for troponin A indicated two classes of binding sites. The Scatchard plots were approximated by assuming that each class contained 4.8 sites/105 g protein and that the high affinity binding constant was equal to 5.4 · 106 M−1 and the low affinity constant was equal to 2 · 105 M−1. Troponin A was purified by column chromatography and it was found that both the calcium binding ability and activity in the assays with troponin B were confined to one component. This was characterized by its high mobility on disc electrophoresis. The purified troponin A was roughly spherical, and had a molecular weight of approximately 18 500. It is unusual in that it contained a high proportion of phenylalanine relative to tyrosine. The excess of negatively charged amino acids would also suggest that at neutral pH it was a polyanion. On a weight basis the purified troponin A bound approximately 50% more calcium than the unpurified troponin A." @default.
• W2090925355 created "2016-06-24" @default.
• W2090925355 creator A5066377959 @default.
• W2090925355 creator A5073744420 @default.
• W2090925355 date "1971-03-01" @default.
• W2090925355 modified "2023-10-17" @default.
• W2090925355 title "Calcium binding by the troponin complex, and the purification and properties of troponin A" @default.
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• W2090925355 doi "https://doi.org/10.1016/0005-2795(71)90286-8" @default.
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