Synthetic substrates and inhibitors for serine proteases from lymphocytes, mast cells, semen, and blood.
The substrate specificity of several serine proteases from cytotoxic T lymphocytes, natural killer cells, mast cells, seminal fluid, and blood plasma has been determined with synthetic peptide thiobenzyl ester and p-nitroanilide substrates. Several new enzymatic activities have been discovered. A variety of inhibitors such as isocoumarins, trifluoromethyl ketones, and peptide chloromethyl ketones were used to study these enzymes and were found to be potent inhibitors.
Powers
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JC
School of Chemistry and Biochemistry, Georgia Institute of Technology, Atlanta 30332.
Odake
S
S
Ueda
T
T
Hudig
D
D
Graves
H C
HC
Kamarei
M
M
Kam
C M
CM
D000595:Amino Acid Sequence; D000818:Animals; D053804:Granzymes; D006801:Humans; D007700:Kinetics; D008214:Lymphocytes / Q000201:enzymology*; D008407:Mast Cells / Q000201:enzymology*; D051379:Mice; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000138:chemical synthesis / Q000378:metabolism; D011994:Recombinant Proteins / Q000378:metabolism; D012661:Semen / Q000201:enzymology*; D012697:Serine Endopeptidases / Q000097:blood / Q000378:metabolism*; D015842:Serine Proteinase Inhibitors / Q000494:pharmacology*; D013379:Substrate Specificity
D009842:Oligopeptides; D011994:Recombinant Proteins; D015842:Serine Proteinase Inhibitors; D053804:Granzymes; D012697:Serine Endopeptidases; C509212:GZMA protein, human