Anomalous dissociation constants for penicillinase and competing substrates
- 1 January 1968
- journal article
- research article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Enzymology
- Vol. 151 (1) , 306-308
- https://doi.org/10.1016/0005-2744(68)90195-2
Abstract
No abstract availableKeywords
This publication has 8 references indexed in Scilit:
- The interaction of penicillinase with penicillins V. Conformative response constantsBiochimica et Biophysica Acta (BBA) - Enzymology, 1967
- The interaction of penicillinase with penicillins IV. Structural aspects of catalytic and non-catalytic interactionsBiochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation, 1965
- The interaction of penicillinase with penicillins: II. Temperature-dependent changes induced in penicillinase by competitive inhibitorsBiochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects, 1963
- The Nature of Resistance of A Penicillin to Hydrolysis by PenicillinaseJournal of Pharmacy and Pharmacology, 1962
- The interaction of penicillinase with penicillins I. Effect of substrates and of a competitive inhibitor on native and urea-treated enzymeBiochimica et Biophysica Acta, 1962
- The determination of enzyme inhibitor constantsBiochemical Journal, 1953
- A Method for Determining the Ratio of the Michael is Constants of an Enzyme with Respect to Two SubstratesNature, 1949
- The Determination of Enzyme Dissociation ConstantsJournal of the American Chemical Society, 1934