title: A purification and some properties of two proteases from papaya latex.
abstract: Two proteases, one of which is papaya peptidase A and the other a previously unknown enzyme in papaya latex have been purified to homogeneity in a simple two stage process. Both are markedly less reactive than papain or chymopapain. Each has a molecular weight of 24,000, N-terminal sequences commencing Leu-Pro-Glu, and contains no carbohydrate. Their amino acid compositions differ for several residues. The essential -SH groups of the enzymes examined appear to be 'masked' in the native state.
mesh_terms: D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D002845:Chromatography; D010450:Endopeptidases / Q000302:isolation & purification*; D008970:Molecular Weight; D010446:Peptide Fragments; D010944:Plants / Q000201:enzymology*
chemical_list: D000596:Amino Acids; D010446:Peptide Fragments; D010450:Endopeptidases