| 摘要 |
A yeast PPIase characterized by possessing following properties: (1) acting on and isomerizing the bond Xaa-Pro (wherein Xaa stands for any amino acid and Pro stands for L-proline), (2) exhibiting a single molecular weight of about 17,000 daltons in the sodium dodecyl sulfate-polyacrylamide concentration gradient gel electrophoresis, (3) exhibiting a single isoelectric point of about 6.2 in the isoelectric focusing, and (4) inhibited by CsA; an E. coli PPIase- beta characterized by possessing the following properties: (1) acting on and isomerizing the bond Xaa-Pro (wherein Xaa stands for any amino acid and Pro for L-proline), (2) exhibiting a single molecular weight of about 20,000 daltons in the sodium dodecyl sulfate-polyacrylamide concentration gradient gel electrophoresis, (3) exhibiting a single isoelectric point of about 5.0 in the isoelectric focusing, and (4) no being inhibited by CsA; an E. coli PPIase- alpha characterized by possessing the following properties: (1) acting on and isomerizing the bond Xaa-Pro (wherein Xaa stands for any amino acid and Pro for L-proline), (2) exhibiting a single molecular weight of about 22,000 daltons in the sodium dodecyl sulfate-polyacrylamide concentration gradient gel electrophoresis, (3) exhibiting a single isoelectric point of about 9.7 in the isoelectric focusing, and (4) not being inhibited by CsA.
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