Abstract
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.
| Original language | English |
|---|---|
| Pages (from-to) | 729-732 |
| Number of pages | 4 |
| Journal | Journal of Biochemistry |
| Volume | 112 |
| Issue number | 6 |
| Publication status | Published - 1992 Dec |
| Externally published | Yes |
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ASJC Scopus subject areas
- Statistics, Probability and Uncertainty
- Applied Mathematics
- Physiology (medical)
- Radiology Nuclear Medicine and imaging
- Molecular Biology
- Biochemistry
Cite this
Purification and characterization of a possible protooncogene fjln product, P59fyn, from a rat brain particulate fraction. / Miyauchi, Takahiro; Ariki, Masahiro; Usui, Hirofumi; Senba, Kentaro; Matsuzawa, Yumiko; Yamamoto, Tadashi; Toyoshima, Kumao; Takeda, Masao.
In: Journal of Biochemistry, Vol. 112, No. 6, 12.1992, p. 729-732.Research output: Contribution to journal › Article
}
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 - Senba, Kentaro
AU - Matsuzawa, Yumiko
AU - Yamamoto, Tadashi
AU - Toyoshima, Kumao
AU - Takeda, Masao
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
M3 - Article
VL - 112
SP - 729
EP - 732
JO - Journal of Biochemistry
JF - Journal of Biochemistry
SN - 0021-924X
IS - 6
ER -