An alternative quenched fluorescence substrate for Pz-peptidase.
7-Methoxycoumarin-3-carboxylyl-Pro-Leu-Gly-Pro-D-Lys(2,4-dinitr oph enyl) is introduced as a new quenched fluorescence substrate for assaying Pz-peptidase (also known as soluble metallo-endopeptidase and endo-oligopeptidase). The value of Km for partially purified Pz-peptidase from rat muscle was 8.6 microM. High protein concentrations did not interfere with the assay, so that for the first time continuous assays of Pz-peptidase in crude tissue extracts became possible.
Biochemistry Department, Strangeways Research Laboratory, Cambridge, United Kingdom.
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U
Tisljar
C G
CG
Knight
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AJ
Barrett
D000595:Amino Acid Sequence; D055598:Chemical Phenomena; D002621:Chemistry; D010450:Endopeptidases / Q000032:analysis*; D005453:Fluorescence; D006868:Hydrolysis; D007700:Kinetics; D008666:Metalloendopeptidases; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000378:metabolism*; D013379:Substrate Specificity
D009842:Oligopeptides; C064546:7-methoxycoumarin-3-carboxylyl-prolyl-leucyl-glycyl-prolyl-lysyl-2,4-dinitrophenyl; D010450:Endopeptidases; D008666:Metalloendopeptidases; C022510:thimet oligopeptidase