Amino acid sequence of the active site of human pseudocholinesterase |
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Authors: | Kunio Yamato I-Yih Huang Helmut Muensch Akira Yoshida Heinz-Werner Goedde Dharam P Agarwal |
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Institution: | 1. Department of Biochemical Genetics, City of Hope Research Institute, 91010, Duarte, California 2. Institute of Human Genetics, University of Hamburg, Hamburg, Germany
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Abstract: | The usualE 1 u and atypicalE 1 a human pseudocholinesterases (acylocholine acylhydrolase, EC 3.1.1.8) were purified to homogeneity. The active-site serine residue was conjugated with diisopropyl fluorophosphate and digested with trypsin. The tryptic peptide containing the active site was isolated by gel filtration followed by two-dimensional paper chromatography and electrophoresis. The amino acid sequence of the active site peptide obtained from the usualE 1 u enzyme was found to be Gly-Glu-Ser-Ala-Gly-Ala-Ser-Ala-Val-Ser-Leu. A remarkable structural homology exists between the human and the horse enzymes in their active sites. From the difference in electrophoretic mobility of the active-site peptides obtained from the usual and atypical enzymes, the probable structure of the atypical human enzyme was deduced as Gly-His-Ser-Ala-Gly-Ala-Ser-Ala-Val-Ser-Leu. |
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