PRIMARY STRUCTURE OF THE BASIC NUCLEAR PROTEIN FROM SPERMATOZOA OF MOLLUSC ILLEX ARGENTINUS AND ITS COMPARISON WITH STRUCTURES OF SPERMATIC PROTEINS OF OTHER ANIMALS

L. A. OSADCHUK, N. B. LEVINA*, I. N. TELEZHINSKAYA*, S. N. KHRAPUNOV, G. D. BERDYSHEV, N. A. ALDANOVA*

T. G. Shevchenko Kiev State University, Kiev; *M. M. Shemyakin Institute of Bioorganic Chemistry, Academy of Sciences of the USSR, Moscow

Abstract: The spermatic protein of chromatin I₂ of squid Illex argentinus was separated by HPLC into two components I_2-1 and I_2-2. Amino acid sequences of the major portion of protein I_2-1 (52 residues) and the N-terminal sequence of protein I_2-2 (21 residues) were determined. Arginines in protein I_{2- 1} are arranged in clusters typical of protamines; the first cluster is in the N-terminus, the longest heterogeneous hasic cluster is in the central part of the protein chain, the C-terminal part of the molecule contains two clusters of three hydroxyamino acids each. The N-terminal sequences of illexins 1_{2- 1} and I_2-2 (1 – 14 residues) are highly homologous. Homologous regions were found in illexin 1^, tun-nin of tuna fish and avian gallin thus defining the notion of proteins of an intermediate type from mollusc spermatozoa chromatin exemplified by the squid protamine-like protein.

Russian Journal of Bioorganic Chemistry 1990, 16 (4):448-456

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