A serine endopeptidase (SEP) was found to be possibly involved in the degra
dation of storage proteins in cotyledons of germinated Vigna mungo seeds. S
EP activity was separated into two isoforms by CM-cellulose column chromato
graphy. These forms, termed SEP-I and SEP-II, showed endopeptidase activiti
es even at acidic pH, suggesting that SEPs are unique serine endopeptidases
, since most serine proteases are optimum at neutral pH.