Substrate activation of porcine pancreatic kallikrein by N.alpha. derivatives of arginine 4-nitroanilides
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00390a022
Reference30 articles.
1. Refined 2 Å X-ray crystal structure of porcine pancreatic kallikrein A, a specific trypsin-like serine proteinase
2. Inhibitory effects of sodium and other monovalent cations on purified versus membrane-bound kallikrein.
3. Refined 2.5 Å X-ray crystal structure of the complex formed by porcine kallikrein A and the bovine pancreatic trypsin inhibitor
4. [24] Pig Pancreatic Kallikreins A and B
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1. Specificity of S'1 and S'2 subsites of human tissue kallikrein using the reactive-centre loop of kallistatin: the importance of P'1 and P'2 positions in design of inhibitors;Biochemical Journal;2003-05-01
2. Kinetic Peculiarities of Human Tissue Kallikrein: 1—Substrate Activation in the Catalyzed Hydrolysis of H--Valyl--leucyl--arginine 4-Nitroanilide and H--Valyl--leucyl--lysine 4-Nitroanilide; 2—Substrate Inhibition in the Catalyzed Hydrolysis of Nα-p-Tosyl--arginine Methyl Ester;Archives of Biochemistry and Biophysics;2002-04
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4. Specificity of human tissue kallikrein towards substrates containing Phe‒Phe pair of amino acids;Biochemical Journal;1999-04-15
5. Functional characterization ofEscherichia coliinorganic pyrophosphatase in zwitterionic buffers;European Journal of Biochemistry;1999-03
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