PMID: 39605Jun 6, 1979

The solubilisation of the membrane-bound D-alanyl-D-alanine carboxypeptidase of Bacillus coagulans NCIB 9365

Biochimica Et Biophysica Acta
H A McArthur, P E Reynolds


Protoplast membranes and the particulate D,D-carboxypeptidase of Bacillus coagulans NCIB 9365 were extremely resistant to disruption by either detergents or urea. A combination of urea and the non-ionic detergent Genapol X-100 was required to achieve a significant solubilisation of membrane protein and D,D-carboxypeptidase in an active form; the pH optimum for this treatment was pH 7.5. Solubilisation of the enzyme was accompanied by a two-fold enhancement of activity. Kinetic results indicated that the enhancement may be due to an alteration in the conformation of the enzyme following disruption of membrane structure.


Mar 1, 1987·Journal of the American College of Cardiology·N C Flowers
Oct 1, 1973·Proceedings of the National Academy of Sciences of the United States of America·J N Umbreit, J L Strominger
May 10, 1974·Annals of the New York Academy of Sciences·J M GhuysenA Marquet
Dec 1, 1972·Proceedings of the National Academy of Sciences of the United States of America·P M Blumberg, J L Strominger
Apr 8, 1974·Biochemical and Biophysical Research Communications·S Mookerjea, J W Yung
Apr 1, 1969·Proceedings of the National Academy of Sciences of the United States of America·Y Hatefi, W G Hanstein

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