Isolation and characterization of enzymes hydrolyzing chymotrypsin synthetic substrate (Enzyme I) and trypsin synthetic substrate (Enzyme II) from the envelope of Capnocytophaga gingivalis.
Enzymes hydrolyzing chymotrypsin synthetic substrate and trypsin synthetic substrate, referred to as Enzyme I and Enzyme II, respectively, were found in the envelope fraction of Capnocytophaga gingivalis (ATCC 33624). Detergent extraction of both enzymes were purified by gel filtration, ion exchange chromatography, and affinity chromatography. The Enzyme I was a serine-containing metallo enzyme with a molecular mass of 77 kDa. The molecular mass of the Enzyme II was 83 kDa, and it was inhibited by tosyl-L-lysine chloromethyl ketone and leupeptin, and thus may be related to trypsin.
Shibata
Y
Y
Department of Oral Microbiology, Matsumoto Dental College, Nagano-Ken, Japan.
Fujimura
S
S
Nakamura
T
T
D000595:Amino Acid Sequence; D000626:Aminopeptidases / Q000037:antagonists & inhibitors / Q000302:isolation & purification / Q000378:metabolism*; D002206:Capnocytophaga / Q000201:enzymology*; D002462:Cell Membrane / Q000201:enzymology; D004795:Enzyme Stability; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D008670:Metals / Q000494:pharmacology; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009842:Oligopeptides / Q000737:chemistry; D013379:Substrate Specificity
D008670:Metals; D009842:Oligopeptides; D000626:Aminopeptidases