Please use this identifier to cite or link to this item: http://lib.jncasr.ac.in:8080/jspui/handle/10572/507
Title: Characterization of the zinc-metalloprotein nature of rat spermatidal protein TP2
Authors: Kundu, Tapas K
Rao, M R S
Keywords: Spermatidal Transition Protein Tp2
(65)Zinc Blotting
Secondary Structure
Secondary-Structure
Sperm
Sequence
Issue Date: 29-Aug-1994
Publisher: Elsevier Science BV
Citation: FEBS Letters 351(1), 6-10 (1994)
Abstract: Spermatidal 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.
Description: Restricted Access
URI: http://hdl.handle.net/10572/507
Other Identifiers: 0014-5793
Appears in Collections:Research Papers (M.R.S. Rao)

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