Is sperminogen a modified proacrosin? Isolation, purification, and partial characterization of low-molecular-mass boar proacrosin.
Low-molecular-mass zymogen was extracted from boar spermatozoa together with proacrosin using 10% acetic acid supplemented with 10% glycerol, and was purified by the sequential use of gel filtration on Sephadex G-75 and (FPLC) reversed-phase chromatography. LMM zymogen represented approximately 5% of the latent trypsin-like activity present in the sperm extract. SDS-PAGE indicated a molecular mass of 33 kDa. The zymogen reacted with both mouse monoclonal and rabbit polyclonal antibodies to boar acrosin. Determination of the N-terminal sequence of 34 amino-acid residues revealed its identity with the known N-terminal sequence of boar proacrosin.
Cechová
D
D
Max-Planck-Institut für Biochemie, Martinsried.
Töpfer-Petersen
E
E
Zucker
A
A
Jonáková
V
V
D000176:Acrosin / Q000032:analysis / Q000302:isolation & purification*; D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis*; D000818:Animals; D004792:Enzyme Precursors / Q000032:analysis / Q000302:isolation & purification*; D008297:Male; D008969:Molecular Sequence Data; D012697:Serine Endopeptidases / Q000302:isolation & purification*; D013094:Spermatozoa / Q000201:enzymology*; D013552:Swine
D000596:Amino Acids; D004792:Enzyme Precursors; D012697:Serine Endopeptidases; C022438:proacrosin; D000176:Acrosin