Isolation of the Boar Sperm Acrosin Peptide Released during the Conversion of α-Form into β-Form

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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 (lingt 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.

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