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- W2326514938 abstract "The sperm proteinase acrosin occurs in several enzymatically active forms which differ from each other in molecular mass. The high-molecular-mass alpha-form (53 kDa) is converted into the low-molecular-mass beta-form (38 kDa) by auto-proteolysis. As these two forms possess identical N-termini and identical A-chains (light chains) the difference must reside in the C-terminal parts of their B-chains (heavy chains). It could be demonstrated by gel electrophoresis that on incubation of alpha-acrosin, in addition to beta-acrosin, a main degradation product of approx. 18 kDa was formed. This fragment was isolated by gel filtration chromatography. The amino-acid composition of the fragment corresponded to the difference between that of alpha-acrosin and of beta-acrosin, and showed a strikingly high proportion of proline. It is suggested that this hydrophobic segment from the C-terminal region of alpha-acrosin accounts for the special membrane-associating property of the enzyme." @default.
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- W2326514938 date "1989-01-01" @default.
- W2326514938 modified "2023-09-26" @default.
- W2326514938 title "Isolation of the Boar Sperm Acrosin Peptide Released during the Conversion of α-Form into β-Form" @default.
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- W2326514938 doi "https://doi.org/10.1515/bchm3.1989.370.1.323" @default.
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