Fawell S E, Higgins S J
Department of Biochemistry, University of Leeds, U.K.
Mol Cell Endocrinol. 1987 Sep;53(1-2):149-52. doi: 10.1016/0303-7207(87)90201-2.
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.