TY - JOUR
T1 - Purification and characterization of a possible protooncogene fjln product, P59fyn, from a rat brain particulate fraction
AU - Miyauchi, Takahiro
AU - Ariki, Masahiro
AU - Usui, Hirofumi
AU - Semba, Kentaro
AU - Matsuzawa, Yumiko
AU - Yamamoto, Tadashi
AU - Toyoshima, Kumao
AU - Takeda, Masao
N1 - Copyright:
Copyright 2018 Elsevier B.V., All rights reserved.
PY - 1992/12
Y1 - 1992/12
N2 - Four tyrosine-protein kinases that reacted with antibodies specific to p62c-yes, p60c-src, p60c-src, and p59fyn, respectively, were solubilized from a rat brain particulate fraction and separated by casein-Toyopearl column chromatography. Possible p59fyn, with a pI of 6.5, was purified 490-fold as a single 69-kDa protein band on SDS-PAGE. The purified enzyme contained almost no phosphotyrosine residues but was autophosphorylated with Mg2+-·ATP exclusively at tyrosine residues, with a concomitant increase in the kinase activity toward tyrosine-glutamate (1 : 4) copolymers. The rate of the copolymer phosphorylation was proportional to the square of the enzyme concentration, suggesting activation through intermolecular catalysis. In the presence of Mn2+, however, the reaction showed a firstorder dependence on the enzyme concentration.
AB - Four tyrosine-protein kinases that reacted with antibodies specific to p62c-yes, p60c-src, p60c-src, and p59fyn, respectively, were solubilized from a rat brain particulate fraction and separated by casein-Toyopearl column chromatography. Possible p59fyn, with a pI of 6.5, was purified 490-fold as a single 69-kDa protein band on SDS-PAGE. The purified enzyme contained almost no phosphotyrosine residues but was autophosphorylated with Mg2+-·ATP exclusively at tyrosine residues, with a concomitant increase in the kinase activity toward tyrosine-glutamate (1 : 4) copolymers. The rate of the copolymer phosphorylation was proportional to the square of the enzyme concentration, suggesting activation through intermolecular catalysis. In the presence of Mn2+, however, the reaction showed a firstorder dependence on the enzyme concentration.
UR - http://www.scopus.com/inward/record.url?scp=0027102391&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0027102391&partnerID=8YFLogxK
U2 - 10.1093/oxfordjournals.jbchem.a123966
DO - 10.1093/oxfordjournals.jbchem.a123966
M3 - Article
C2 - 1338328
AN - SCOPUS:0027102391
VL - 112
SP - 729
EP - 732
JO - Journal of Biochemistry
JF - Journal of Biochemistry
SN - 0021-924X
IS - 6
ER -