Author:
Matheson A. T.,Murayama T.
Abstract
When lysozyme–EDTA spheroplasts are formed from Escherichia coli cells, only a small fraction of the total peptidase activity of the cell is released into the supernatant fluid under conditions where ribonuclease is quantitatively released. Purification of the released peptidase on DEAE-Sephadex gives two fractions. The peptidase in one fraction shows the same substrate specificity, metal ion requirements, and chromatographic properties as the ribosomal peptidase of the cell; the peptidase in the other fraction shows the same properties as the soluble peptidases of the cell. The ribosomal peptidase does not belong to the group of hydrolytic enzymes that are released when E. coli cells are converted into spheroplasts.
Publisher
Canadian Science Publishing
Cited by
26 articles.
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