A new latent arginine esteropeptidase from human submaxillary gland.
One of the arginine esteropeptidases in human submaxillary gland was purified from microsomal membranes. The enzyme is inactive in membranes and requires trypsin treatment for its full activation. The trypsin-activated enzyme was purified to homogeneity. Its molecular weight was determined to be 94,000 by SDS-polyacrylamide gel electrophoresis. Among various substrates examined, the obtained enzyme exhibited high specific activities toward Tos-Arg-OMe (esterolysis) and D-Ile-Pro-Arg-pNA (amidolysis). The enzyme was inhibited by some serine proteinase inhibitors, whereas inhibitors of other types of proteinases did not affect or only scarcely affected it. The enzyme appears to be distinct from other arginine esteropeptidases previously described.
Watanabe
Y
Y
Department of Clinical Biochemistry, Hokkaido Institute of Pharmaceutical Sciences, Japan.
Suzuki
C
C
Fujimoto
Y
Y
D000577:Amides / Q000378:metabolism; D000595:Amino Acid Sequence; D004591:Electrophoresis, Polyacrylamide Gel; D004789:Enzyme Activation; D004792:Enzyme Precursors / Q000302:isolation & purification*; D004952:Esters / Q000378:metabolism; D006801:Humans; D007705:Kinins / Q000378:metabolism; D001121:Lysine Carboxypeptidase / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D008565:Membrane Proteins / Q000302:isolation & purification; D008861:Microsomes / Q000378:metabolism; D008969:Molecular Sequence Data; D013363:Submandibular Gland / Q000201:enzymology*; D013379:Substrate Specificity; D014357:Trypsin / Q000378:metabolism
D000577:Amides; D004792:Enzyme Precursors; D004952:Esters; D007705:Kinins; D008565:Membrane Proteins; D001121:Lysine Carboxypeptidase; D014357:Trypsin