Kundu, TK and Rao, MRS (1994) Characterization of the zinc-metalloprotein nature of rat spermatidal protein TP2. In: FEBS letters, 351 (1). pp. 6-10.
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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.
|Item Type:||Journal Article|
|Additional Information:||Copyright of this article belongs to Elsevier science.|
|Keywords:||Spermatidal transition protein TP2; 65Zinc blotting; Secondary structure|
|Department/Centre:||Division of Biological Sciences > Biochemistry|
|Date Deposited:||25 Mar 2011 04:56|
|Last Modified:||25 Mar 2011 04:56|
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