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Is sperminogen a modified proacrosin? Isolation, purification, and partial characterization of low-molecular-mass
D Cechová1, E Töpfer-Petersen, A Zucker
1Max-Planck-Institut für Biochemie, Martinsried.
Biological Chemistry Hoppe-Seyler
|April 1, 1990
Abstract:
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.