• BMB Reports
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• 제30권6호
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• pp.448-452
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• 1997

Polyclonal antibody of the boar sperminogen was used to characterize the boar sperm proteinase sperminogen. Boar sperminogen was purified from the acid extracts of the washed epididymal spermatozoa by gel filtration through a Sephadex G-100 column. followed by preparative SDS-PAGE. The sperminogen band was sliced out and was eluted from the gel matrix. The purified sperminogen was used to produce the polyclonal antibody of the boar sperminogen. When characterized on a Western blot, the final preparation of sperminogen appeared as a homogenous protein with a molecular weight of 32 kDa. The relative migration of sperminogen was distinctly different from the major components of the proacrosin-acrosin system as well as all the observable proacrosin activation by-products detected on the Western blot. The sperminogen antibody, however. cross-reacted with the proacrosin-acrosin system.

• BMB Reports
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• 제33권6호
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• pp.510-513
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• 2000

Boar sperminogen was purified from the acid extracts of the washed epididymal spermatozoa by gel filtration through a Sephadex G-100 column, followed by preparative SDS-PAGE. The 32 kDa sperminogen band was sliced out from the preparative SDS-PAGE and 32 kDa sperminogen was eluted from the gel matrix. The purified 32 kDa sperminogen was subjected to amino acid composition analysis. The amino acid composition of the 32 kDa boar sperminogen showed significant differences from that of either boar proacrosin or ${\beta}-acrosin$, which signifies that 32 kDa sperminogen might not be a breakdown product of proacrosin-acrosin system and that the 32 kDa sperminogen is a different protein from proacrosin-acrosin system.

• 한국동물학회:학술대회논문집
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• 한국동물학회 2001년도 한국생물과학협회 학술발표대회
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• pp.202.3-203
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• 2001

No Abstract, See Full Text

• 한국동물학회:학술대회논문집
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• 한국동물학회 2001년도 한국생물과학협회 학술발표대회
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• pp.203.1-203
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• 2001

No Abstract, See Full Text

• Animal cells and systems
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• 제5권3호
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• pp.199-203
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• 2001

Sperminogen was purified from the acid extracts of boar spermatozoa and partial peptide sequence of the 34-36 kd sperminogen was determined. Acid extracts of boar spermatozoa was gel-filtered through Sephadex G-75, and the 34-36 kd sperminogen was purified by preparative SDS-PAGE. The sperminogen bands were sliced out, and 34-36 kd sperminogen were eluted from the gel fragments and was subjected to peptide sequencing. Since the amino termini were blocked for Edman degradation method, internal amino acid sequences of the eluted 34-36 kd sperminogen were obtained from CNBr-digested peptides of sperminogen. Among several bands resolved on tricine SDS-PAGE, 14, 22 and 26 kd peptides were subjected to peptide sequencing. The ana1yzed amino acid sequences of the 26 and 22 kd peptides showed high homologies with that of the zona pellucida binding protein, Sp38, and the analyzed amino acid sequence of the 14 kd peptide showed neither sequence homology nor similarity with any known proteins.