Partial Amino Acid Sequences of Peptidyl-Prolyl Isomerases ofFusarium sporotrichioides.
Peptidyl-proprylyl cis-trans isomerase (PPIase) activity was observed from crude extract of Fusarium 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 from Neurospora 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. Copyright 1995 S. Karger AG, Basel
Fukaya
N.
N
Department of Microbiology I, School of Veterinary Medicine, Azabu University, Kanagawa, Japan.
Chow
L.-P.
LP
Sugiura
Y.
Y
Tsugita
A.
A
Ueno
Y.
Y
Tabuchi
K.
K