Abstract
The amino acid sequence of mesentericopeptidase, originating from a strain of B. mesentericus, has been determined in part (95% of total) by: a) direct sequencing of intact protein and peptides obtained by cleavage with cyanogen bromide, trypsin and S. aureus protease, b) indirectly by comparison of partially characterized chymotryptic peptides with the sequence of subtilisin amylosacchariticus. Mesentericopeptidase belongs to the family of subtilisins related to subtilisin BPN'/Novo and it is highly homologous with subtilisin amylosacchariticus. A minor error in the sequences of subtilisin Novo and subtilisin amylosacchariticus has been corrected.
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