Isolation of the boar sperm acrosin peptide released during the conversion of alpha-form into beta-form.
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.
Institute of Molecular Genetics, Czechoslovak Academy of Sciences, Praha.
B
B
Zelezná
D
D
Cechová
A
A
Henschen
D000176:Acrosin / Q000302:isolation & purification*; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D007536:Isomerism; D008297:Male; D010455:Peptides / Q000302:isolation & purification*; D012697:Serine Endopeptidases / Q000302:isolation & purification*; D013094:Spermatozoa / Q000378:metabolism*; D013552:Swine
D000596:Amino Acids; D010455:Peptides; D012697:Serine Endopeptidases; D000176:Acrosin