Nonkallikrein arginine endopeptidase in the human submaxillary gland: purification and characterization of the enzyme.
The two major species of arginine endopeptidase present in the soluble fraction of human submaxillary gland are glandular kallikrein and another enzyme tentatively named nonkallikrein arginine endopeptidase. In this study, we purified the latter enzyme to homogeneity and examined its catalytic properties. The newly found enzyme was clearly distinguishable from human tissue kallikrein in its molecular nature, action toward various synthetic substrates, and kinin-generated activity. The specificity of the action of the enzyme was further investigated using various basic amino acid-containing peptides as model substrates. HPLC analysis of peptide fragments produced, followed by their amino acid analysis, revealed that the enzyme preferentially hydrolyzed the Arg-Arg or Arg-Lys bonds in dynorphins A 1-10, 1-9, and 1-8, beta-neoendorphin, adenorphin, and neurotensin.
Department of Clinical Biochemistry, Hokkaido Institute of Pharmaceutical Sciences, Japan.
Y
Y
Watanabe
M
M
Suzuki
Y
Y
Fujimoto
D000595:Amino Acid Sequence; D002384:Catalysis; D005591:Chemical Fractionation; D006801:Humans; D007610:Kallikreins / Q000032:analysis*; D007705:Kinins / Q000378:metabolism; D008969:Molecular Sequence Data; D012697:Serine Endopeptidases / Q000302:isolation & purification*; D012995:Solubility; D013363:Submandibular Gland / Q000201:enzymology*; D013379:Substrate Specificity
D007705:Kinins; D007610:Kallikreins; D012697:Serine Endopeptidases; C060325:arginine endopeptidase