Galactosyltransferase: confirmation of equilibrium-ordered mechanism. |
| |
Authors: | C R Geren L M Geren K E Ebner |
| |
Institution: | Department of Organic Chemistry, The Weizmann Institute of Science, Rehovot, Israel |
| |
Abstract: | A thermostable protein that strongly inhibits the soluble D-alanine carboxypeptidase was isolated from a cell-free extract of . The inhibitor was purified 140-fold by heat treatment, selective precipitation at pH 4.5, ion exchange chromatography on DEAE-cellulose and gel chromatography on Sephadex G-100. Inhibition of soluble D-alanine carboxypeptidase by this inhibitor is reversed by cations such as Mg++ or Na+ and abolished by digestion of the inhibitor with proteolytic enzymes. The inhibitor does not affect either the particulate D-alanine carboxypeptidase of or the growth of the bacteria. |
| |
Keywords: | MurNAc N-acetylmuramic acid α ε - mesodiaminopimelic acid DACI D-alanine carboxypeptidase inhibitor |
本文献已被 ScienceDirect 等数据库收录! |