CRYSTALLINE BACTERIAL PROTEINASE:VI. PHOSPHOPEPTIDES FROM A BACTERIAL PROTEINASE INHIBITED BY DIISOPROPYL FLUOROPHOSPHATE

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The phosphorus content of a bacterial proteinase, BPN', which had been inhibited by DFP, was analyzed and the site of attachment of the phosphorus, and structure of the adjacent peptide examined. One mole of phosphorus was present per mole of protein. It was shown that Ser must be the amino acid residue binding the phosphorus of DFP. The neighboring peptide con-tained Gly, Glu or Glu(NH2), and some other amino acids.<br> The author wishes to express his thanks to Prof. K. O kunuki and Dr. B. Hagihara for their kind advice during this work. I would like to thank Dr. M. L. Huggins, Research Lab., Eastman Kodak Co., Rochester, N. Y., for a gift of p-Semidine, and I am grateful to Nagase Co. Ltd. for kindly supplying the enzyme source materials.

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