Purification and partial peptide sequence analysis of the boar proacrosin binding protein

Authors
Citation
K. Huh et Lsh. Yi, Purification and partial peptide sequence analysis of the boar proacrosin binding protein, MOL REPROD, 54(1), 1999, pp. 76-80
Citations number
12
Categorie Soggetti
Cell & Developmental Biology
Journal title
MOLECULAR REPRODUCTION AND DEVELOPMENT
ISSN journal
1040452X → ACNP
Volume
54
Issue
1
Year of publication
1999
Pages
76 - 80
Database
ISI
SICI code
1040-452X(199909)54:1<76:PAPPSA>2.0.ZU;2-I
Abstract
Boar proacrosin binding protein has been purified and the partial peptide s equence of the CNBr-digested proacrosin binding protein has been determined . Proacrosin binding protein was purified as a proacrosin and proacrosin bi nding protein complex from the acid extracts of boar spermatozoa through ge l filtration. After the proacrosin binding protein was dissociated from pro acrosin by freeze-thaw method, the proacrosin binding protein was purified through gel filtration. Fractions containing the proacrosin binding protein were pooled and were concentrated by lyophilization and then subjected to CNBr digestion. Four major CNBr-digested peptides were subjected to N-termi nal peptide sequencing. All four showed the same N-terminus sequence. (C) 1 999 Wiley-Liss, Inc.