Literature DB >> 6418209

Thermal denaturation of native and cross-linked Bacillus cereus 569/H beta-lactamase I.

L D Arnold, T Viswanatha.   

Abstract

Thermal denaturation of native and internally cross-linked Bacillus cereus 569/H beta-lactamase I (beta-lactamhydrolase, EC 3.5.2.6) was investigated using differential scanning calorimetry. Application of temperature-scanning kinetics provided an estimate of various activation parameters for the denaturation process. Evidence is presented to indicate that subtle temperature-induced conformational changes preceding gross denaturation are sufficient to cause inactivation of the enzyme.

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Year:  1983        PMID: 6418209     DOI: 10.1016/0167-4838(83)90252-2

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  2 in total

1.  Potentiation of thermal inactivation of glyceraldehyde-3-phosphate dehydrogenase by photodynamic treatment. A possible model for the synergistic interaction between photodynamic therapy and hyperthermia.

Authors:  C Prinsze; T M Dubbelman; J Van Steveninck
Journal:  Biochem J       Date:  1991-06-01       Impact factor: 3.857

2.  Interaction of beta-lactamases I and II from Bacillus cereus with semisynthetic cephamycins. Kinetic studies.

Authors:  J Martin Villacorta; P Arriaga; J Laynez; M Menendez
Journal:  Biochem J       Date:  1991-10-01       Impact factor: 3.857

  2 in total

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