CRYSTALLINE BACTERIAL PROTEINASE:VI. PHOSPHOPEPTIDES FROM A BACTERIAL PROTEINASE INHIBITED BY DIISOPROPYL FLUOROPHOSPHATE
-
- MATSUBARA HIROSHI
- Department of Biology Faculty of Science, Unviersity of Osaka
この論文をさがす
説明
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.
収録刊行物
-
- The Journal of Biochemistry
-
The Journal of Biochemistry 46 (2), 107-112, 1959
The Japanese Biochemical Society
- Tweet
詳細情報 詳細情報について
-
- CRID
- 1570572703174188928
-
- NII論文ID
- 130003536334
-
- ISSN
- 0021924X
-
- 本文言語コード
- en
-
- データソース種別
-
- CiNii Articles