Partial amino acid sequences of peptidyl-prolyl isomerases ofFusarium sporotrichioides |
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Authors: | Nobuhito Fukaya Lu-Ping Chow Yoshitsugu Sugiura Akira Tsugita Yoshio Ueno Kiyoshi Tabuchi |
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Institution: | (1) Department of Microbiology I, School of Veterinary Medicine, Azabu University, Kanagawa;(2) Department of Toxicology and Microbial Chemistry, Faculty of Pharmaceutical Sciences, Science University of Tokyo, Tokyo;(3) Research Institute for Biosciences, Science University of Tokyo, 2669 Yamazaki, 278 Noda, Japan |
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Abstract: | Peptidyl-proprylyl cis-trans isomerase (PPIase) activity was observed from crude extract ofFusarium sporotrichioides. Proteins from this fungi were separated by two-dimensional polyacrylamide gel electrophoresis and more than one thousand protein spots were separated. Two cytosolic PPIases were found by the N-terminal sequencing from the two separated spots. The N-terminal 41 residues of the major protein spot showed high sequence identity (63.4%) with PPIase fromNeurospora crassa. This protein was designated as PPIase a, having an apparent molecular mass of 20 kD and pI 7.0. The minor other protein spot, having a similar molecular mass but distinguishable pI 6.4, was also sequenced and the N-terminal twenty residues were almost identical to PPIase a and was designated as PPIase b. |
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Keywords: | Fusarium sporotrichioides Peptidyl-prolyl isomerase Partial amino acid sequence |
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