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dc.contributor.authorKundu, Tapas K-
dc.contributor.authorRao, M R S-
dc.identifier.citationFEBS Letters 351(1), 6-10 (1994)en_US
dc.descriptionRestricted Accessen_US
dc.description.abstractSpermatidal transition protein, TP2, was purified from rat testes by Hg-affinity chromatography. The present study reports the details of the zinc-metalloprotein nature of TP2 by employing the Zn-65-blotting technique. Chemical modification of cysteine by iodoacetic acid, and histidine by diethylpyrocarbonate, resulted in a near complete inhibition of Zn-65-binding to TP2. The (65)Zinc-binding was localized to the V8 protease-derived N-terminal two-third polypeptide fragment. Circular dichroism spectroscopy studies of TP2 (zinc pre-incubated) and its V8 protease-derived polypeptide fragments revealed that the N-terminal fragment has a Type I-beta-turn spectrum, while the C-terminal fragment has a small but significant alpha-helical structure. EDTA altered the circular dichroism spectrum of TP2 and the N-terminal fragment (zinc binding domain) but not that of the C-terminal fragment.en_US
dc.publisherElsevier Science BVen_US
dc.rights© 1994 Federation of European Biochemical Societiesen_US
dc.subjectSpermatidal Transition Protein Tp2en_US
dc.subject(65)Zinc Blottingen_US
dc.subjectSecondary Structureen_US
dc.titleCharacterization of the zinc-metalloprotein nature of rat spermatidal protein TP2en_US
Appears in Collections:Research Papers (M.R.S. Rao)

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