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- W2025230978 abstract "A leucylglycine-splitting enzyme from E. coli ribosomes has been purified and its properties studied. The ribosomal proteins were solubilized by disrupting the ribosomal particles in 1 M Tris. As purification proceeded the ionic strength required to keep the proteins in solution steadily decreased until, in the later stages, the enzyme could be fractionated on ion-exchange columns at low ionic strengths. The ribosomal peptidase requires K + or Cs + and Mn 2+ or Mg 2+ for full activity and is inhibited by Na + and Li + . It is completely inhibited by EDTA. The enzyme, which is a basic protein with no absorbancy maximum in the 280 mμ region of the spectrum, has a broad optimum pH range from 7.5 to 9.2. On small-scale preparations over a 1000-fold purification has been obtained." @default.
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- W2025230978 date "1965-10-01" @default.
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- W2025230978 title "PURIFICATION AND PROPERTIES OF A RIBOSOMAL PEPTIDASE FROM ESCHERICHIA COLI B" @default.
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- W2025230978 doi "https://doi.org/10.1139/o65-181" @default.
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