Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
. 1974 Oct;143(1):137-41.
doi: 10.1042/bj1430137.

Conformational changes in the extracellular beta-lactamase I from Bacillus cereus 569/H/9

Conformational changes in the extracellular beta-lactamase I from Bacillus cereus 569/H/9

R B Davies et al. Biochem J. 1974 Oct.

Abstract

1. The thermal denaturation and precipitation of beta-lactamase I from Bacillus cereus 569/H/9 at 60 degrees C are reversible, a soluble and almost fully active enzyme being obtained after solution of the precipitate in 5m-guanidinium chloride or 8m-urea and subsequent removal of the denaturing agent. 2. Inactivation of beta-lactamase I occurs rapidly between 50 degrees and 55 degrees C and is shown by circular-dichroism spectra to be accompanied by an extensive conformational change. 3. A change to a different conformation occurs in 6m-urea. This change is also reversible; refolding with almost complete recovery of enzymic activity occurs within 5min of dilution of the denaturing agent. 4. Inactivation of beta-lactamase I at pH3.0 and 11.0 is also associated with conformational changes, since a proportion of the lost activity is recovered within 5min of adjustment of the pH to 7.0.

PubMed Disclaimer

References

    1. J Biol Chem. 1970 May 10;245(9):2205-12 - PubMed
    1. J Biol Chem. 1970 Jul 25;245(14):3556-60 - PubMed
    1. Biochem J. 1970 Jul;118(3):457-65 - PubMed
    1. Biochim Biophys Acta. 1971 Jun 29;236(3):619-27 - PubMed
    1. Biochem J. 1962 Apr;83:52-63 - PubMed