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- W2016028640 abstract "Digestion of βc-hemocyanin yielded tubular polymers as well as so-called collars. Analysis of the collar fraction revealed that it consisted of two fragments, one having a relative molecular mass of approx. 125 000 and the other a relative molecular mass of approx. 65 000. They were separated using ion-exchange chromatography. The large fragment dissociated around pH 9.5 into two components having a molecular mass of approx. 65 000. Both fragments bound oxygen and displayed heterotropic interactions. The large fragment bound oxygen with a Hill coefficient less than unity under certain conditions. The fragments differed also in amino acid composition, sugar content, spectral parameters, association-dissociation phenomena and ageing. By comparison with fragments obtained after limited proteolysis of tenth molecules, their location in the polypeptide chain was established." @default.
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- W2016028640 date "1981-04-01" @default.
- W2016028640 modified "2023-09-27" @default.
- W2016028640 title "Structural and functional aspects of collar domains of Helix pomatia βc-Hemocyanin" @default.
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- W2016028640 doi "https://doi.org/10.1016/0005-2795(81)90034-9" @default.
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