Amino acid sequence of mouse submaxillary gland renin.

Abstract

The complete amino acid sequences of the H chain and L chain of mouse submaxillary gland renin were determined. The H chain consists of 288 amino acid residues having a MW of 31,036 calculated from the sequence. The L chain contains 48 amino acid residues with a MW of 5458. The sequence of the H chain was determined by automated Edman degradations of the cyanogen bromide peptides and tryptic peptides generated after citraconylation, and other peptides generated therefrom. The sequence of the L chain was derived from sequence analyses of the peptides generated by cyanogen bromide cleavage or by digestion with Staphylococcus aureus protease. The sequences in the active site regions in renin containing 2 catalytically essential aspartyl residues 32 and 215 were found identical with those in pepsin, chymosin and penicillopepsin. Comparison of the amino acid sequence of renin with that of porcine pepsin indicated a 42% sequence identity of the H chain with the amino-terminal and middle regions and a 46% identity of the L chain with the carboxyl-terminal region of the porcine pepsin sequence. Residues identical in renin and pepsin are distributed throughout the length of the molecules, suggesting a similarity in their overall structures.