KINETIC STUDIES OF THE ALKALINE MESENTERICOPEPTIDASE.
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1399-3011.1976.tb02498.x/fullpdf
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1. Three-dimensional Structure of Tosyl-α-chymotrypsin
2. The Aromatic Substrate Binding Site in Subtilisin BPN' and Its Resemblance to Chymotrypsin
3. Binding-catalysis relationship in α-chymotrypsin action as revealed from reversible inhibition study of phenylalkylboronic acids
4. Inhibition of Serine Proteases by Arylboronic Acids
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1. PRIMARY SPECIFICITY OF ALKALINE MESENTERICOPEPTIDASE;International Journal of Peptide and Protein Research;2009-01-12
2. Applications to Biochemical Investigations;Organometallic Compounds and Living Organisms;1984
3. Secondary interactions in mesentericopeptidase-catalyzed hydrolysis of peptide ester and 4-nitroanilide substrates;Archives of Biochemistry and Biophysics;1983-09
4. Bor und spezielle Borverbindungen;BOR in Biologie, Medizin und Pharmazie;1980
5. A study of the alkaline mesentericopeptidase active site by means of peptide chloromethyl ketones;Biochimica et Biophysica Acta (BBA) - Enzymology;1978-11
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