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Identification of phosphotyrosine as a product of epidermal growth factor-activated protein kinase in A-431 cell membranes.

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Ushiro, H., Cohen, S.·1980·Journal of Biological Chemistry

Abstract

Epidermal growth factor (EGF)-enhanced protein kinase activity in plasma membrane preparations of A-431 human epidermoid carcinoma cells was shown to involve the phosphorylation of tyrosine residues. Phosphotyrosine was detected in both endogenous membrane proteins and in histone when added as an exogenous protein substrate. The major phosphorylated amino acid in partial acid hydrolysates of 32P-labeled A-431 membranes was identified as phosphotyrosine on the basis of its identical behavior to authentic phosphotyrosine on paper electrophoresis and thin layer chromatography; its 5-dimethylaminonaphthalene-1-sulfonyl (dansyl) derivative was indistinguishable from that of the authentic compound. Only traces, if any, of phosphoserine or phosphothreonine were detected. [32P]Phosphotyrosine was also detected in pronase digests of 32P-labeled membrane proteins. The EGF receptor . protein kinase complex, which was solubilized with Triton X-100 and purified by EGF affinity chromatography, was shown to phosphorylate tyrosine residues of the isolated membrane protein.

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Metadata

Authors
Ushiro, H., & Cohen, S.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1980-09
Volume
255
Issue
18
Pages
8363-8365
ISSN
0021-9258 (ISSN-L)
OpenAlex
W1524333424
Cited by
1,169
References
0
FWCI
32.41
Type
journal article
Language
en
Open access
hybrid

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CoChat. (2026). Citation check: Identification of phosphotyrosine as a product of epidermal growth factor-activated protein kinase in A-431 cell membranes. https://app.cochat.ai/papers/10.1016/s0021-9258(18)43497-7
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Ushiro, H., & Cohen, S. (1980). Identification of phosphotyrosine as a product of epidermal growth factor-activated protein kinase in A-431 cell membranes. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(18)43497-7

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