Abstract: 212

PURIFICATION AND PARTIAL PEPTIDE SEQUENCE ANALYSIS OF BOAR SPERMINOGEN.

Hyunkyung Yu¹ , Lee SH Yi¹
Dept of Biological Science and Inst for Basic Science, Sungkyunkwan Univ, Suwon 440-746, Korea ¹

Partial peptide sequence of boar 32 kd sperminogen was determined. Boar sperminogen was purified from the acid extracts of boar spermatozoa through gel filtration and preparative SDS-PAGE. Analysis of the gel filtered fractions by gelatin SDS-PAGE showed that sperminogen was composed of three separate proteolytic bands. Among the three bands, the lowest molecular weight band which showed most proteolytic activities upon activation was chosen for further analysis. The fractions containing sperminogen were pooled and freeze-dried. After being resuspended, samples were subjected to preparative SDS-PAGE. The 32 kd sperminogen band was sliced out and electro-eluted. The eluted sperminogen was then subjected to peptide sequencing. Since the N-terminus of the sperminogen was blocked for peptide sequencing by Edman degradation method, the internal amino acid sequence was obtained from the CNBr-digested peptides of the sperminogen. Among the digested peptides, the prominent 29 kd peptide band was analyzed for amino acid sequence. The amino acid sequence of up to 20 amino acids showed a perfect match with that of proacrosin, implying that 32 kd sperminogen is part of the proacrosin-acrosin system. (This work is supported by an MOE Grant, Korea.)

    This abstract is being presented on Monday, August 2 at 8:00 AM to 10:15 AM at CUB 2nd Floor Ballroom.