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. 1980 May 1;187(2):529–532. doi: 10.1042/bj1870529

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

Y Klemes, N Citri
PMCID: PMC1161821  PMID: 6249271

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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