Relaxin amino acid sequence

Relaxin is another peptide that can be extracted from the ovary. The three-dimensional structure of relaxin is related to that of growth-promoting peptides and is similar to that of insulin. Although the amino acid sequence differs from that of insulin, this hormone, like insulin, consists of two chains linked by disulfide bonds, cleaved from a prohormone. It is found in the ovary, placenta, uterus, and blood. Relaxin synthesis has been demonstrated in luteinized granulosa cells of the corpus luteum. 

Amino acid sequences Euplotes raikovi mating pheromones, 154 relaxin, 9 l-92,93r... 

Table I. Amino Acid Sequences of Insulins from Various Species Aligned with the Amino Sequences of IGF and Relaxin... 

Relaxin is a peptide hormone that is synthesized and stored in the corpus luteum and is responsible for the relaxation of the pubic symphysis in mammals prior to parturition. Porcine relaxin (MW 5600) is composed of an A and a B chain linked by disulfide bonds, and its amino acid sequence is consistent with these links having the same disposition as those in insulin (Schwabe et al, 1976 1977 Kwok et a/., 1977) (see Table I). Using its sequence homology with insulin, Bedarkar et al (1977) postulated a three-dimensional structure for relaxin with the crystal structure of insulin as a basis (Fig. 6). A similar model has been proposed by Isaacs et al (1978). 

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