Cross-linking preserves conformational changes induced in penicillinase by its substrates
- 30 April 1980
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 187 (2), 529-532
- https://doi.org/10.1042/bj1870529
Abstract
Exopenicillinase of Bacillus cereus 569/H was cross-linked with toluene 2,4-diisocyanate in the presence of cephalothin, cloxacillin or no substrate. The derivatives show significant differences in susceptibility to inactivation by heat, urea, iodination or proteolysis. Such differences can be predicted from the contrasting effects of these substrates on the conformation of the enzyme.This publication has 16 references indexed in Scilit:
- Acquisition of substrate-specific parameters during the catalytic reaction of penicillinase.Proceedings of the National Academy of Sciences, 1976
- A direct spectrophotometric assay and determination of Michaelis constants for the β-lactamase reactionAnalytical Biochemistry, 1975
- Conformational Adaptability in EnzymesPublished by Wiley ,1973
- Chemical nature of the inactivation of Bacillus cereus penicillinase by iodineBiochimica et Biophysica Acta (BBA) - Protein Structure, 1971
- Determination of free amino groups in proteins by trinitrobenzenesulfonic acidAnalytical Biochemistry, 1966
- DETERMINATION OF PENICILLINASE ACTIVITY.1964
- The Solubility of Amino Acids and Related Compounds in Aqueous Urea SolutionsJournal of Biological Chemistry, 1963
- 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
- On the Formation of Covalent Linkages between Two Protein MoleculesJournal of Biological Chemistry, 1961
- The Effect of Urea and Guanidine Hydrochloride on Activity and Optical Rotation of PenicillinaseJournal of Biological Chemistry, 1960