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Biology Articles » Methods & Techniques » Metabolic Mapping of Proteinase Activity with Emphasis on In Situ Zymography of Gelatinases : Review and Protocols » Table

Table
- Metabolic Mapping of Proteinase Activity with Emphasis on In Situ Zymography of Gelatinases : Review and Protocols

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Table 1 Synthetic substrates with 4-methoxy-2-naphthylamine as leaving group for metabolic mapping of proteases

Substrate
Enzyme
H-Gln Aminopeptidase A
H-Ala Aminopeptidase M
H-Leu
H-Phe
Bz-Arg Cathepsin B
Bz-Val-Lys-Lys-Arg
H-Phe-Pro-Ala-Met
Z-Ala-Arg-Arg
Z-Arg-Arg
Z-Phe-Arg
Z-Val-Lys-Lys-Arg
H-Gly-Arg Cathepsin C
H-Gly-Phe
H-His-Ser
H-Pro-Arg
Bz-Arg-Gly-Phe-Phe-Leu Cathepsin D
Bz-Arg-Gly-Phe-Phe-Pro
H-Arg Cathepsin H
Z-Phe-Arg Cathepsin L
Glu-Ala-Ala-Phe Chymotrypsin
Suc-Phe-Leu-Phe
Z-Pro-Ala-Gly-Pro Collagenases
H-Lys-Ala Dipeptidyl peptidase II
H-Lys-Pro
H-Arg-Arg DPPIII
H-Gly-Pro DPPIV
H-Lys-Pro
Glu-Ala-Ala-Ala Elastases
H-D-Val-Leu-Arg Kallikreins
H-Leu Leucyl aminopeptidase
Glu-Ala-Ala-Phe Neutral endopeptidase
Z-Ala-Ala-Lys Plasmin
Z-Ala-Pro Prolyl endopeptidase
Z-Pro-Phe-His-Leu-Leu-
  Val-Tyr-Ser
Renin
Z-Gly-Pro-Arg Thrombin
Z-Gly-Gly-Arg Tissue-type plasminogen activator
Z-Arg-Arg-Arg Trypsin
Z-Gly-Gly-Arg
Z-Gly-Gly-Arg
Urokinase-type plasminogen activator

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