Primary structure of alpha-clostripain light chain.
The primary structure of light chain of alpha-clostripain was determined by sequence analysis of peptides derived from tryptic digests purified by reverse-phase high-performance liquid chromatography. The 22 isolated tryptic peptides were aligned by peptides derived from chymotryptic and staphylococcal V8 proteinase digests. The light chain contains 133 amino acids residues and has a relative molecular mass of 15400. The prediction of its secondary structure is given.
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D055598:Chemical Phenomena; D002621:Chemistry; D002851:Chromatography, High Pressure Liquid; D002918:Chymotrypsin; D003013:Clostridium / Q000201:enzymology; D003546:Cysteine Endopeptidases; D010450:Endopeptidases; D010446:Peptide Fragments / Q000032:analysis; D012697:Serine Endopeptidases; D014357:Trypsin
D000596:Amino Acids; D010446:Peptide Fragments; D010450:Endopeptidases; D012697:Serine Endopeptidases; D002918:Chymotrypsin; C028344:glutamyl endopeptidase; D014357:Trypsin; D003546:Cysteine Endopeptidases; C019913:clostripain