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Formation of rat copulatory plug: purified seminal vesicle secretory proteins serve as transglutaminase substrates.

作者信息

Fawell S E, Higgins S J

机构信息

Department of Biochemistry, University of Leeds, U.K.

出版信息

Mol Cell Endocrinol. 1987 Sep;53(1-2):149-52. doi: 10.1016/0303-7207(87)90201-2.

Abstract

An in vitro system has been used to study the role of purified rat seminal vesicle proteins in the formation of the copulatory vaginal plug. Proteins II, IV (or S) and V (or F) were each separately coagulated using the transglutaminase in coagulating gland extracts. In each case the coagulum required Ca2+ ions for its formation and was insoluble in denaturing solvents. In experiments with [3H]lysine, proteins II and S incorporated [3H]lysine into glu-lys dipeptide with similar kinetics. Both the N-terminal and C-terminal glutamine residues of protein S participated in the reaction.

摘要

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