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Cross-linking preserves conformational changes induced in penicillinase by its substrates

1980; Portland Press; Volume: 187; Issue: 2 Linguagem: Inglês

10.1042/bj1870529

1470-8728

Yoel Klemes, Nathan Citri,

Mass Spectrometry Techniques and Applications

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.