Identification of phosphorylated 422(aP2) protein as pp15, the 15-kilodalton target of the insulin receptor tyrosine kinase in 3T3-L1 adipocytes.
- 1 December 1988
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 85 (23), 8835-8839
- https://doi.org/10.1073/pnas.85.23.8835
Abstract
[32P]pp15, the [32P]phosphorylated form of a specific cytosolic substrate of the insulin receptor tyrosine kinase, was purified to homogeneity from mouse 3T3-L1 adipocytes incubated with 32Pi. Evidence presented here and previously indicates that pp15 contains a single phosphotyrosine residue. Alkylated [32P]pp15 was subjected to limited digestion with trypsin, after which three incompletely digested tryptic [32P]phosphopeptides were purified for analysis. Amino acid and radiochemical sequence analysis of the [32P]phosphopeptides revealed that pp15 is the phosphorylation product of 422(aP2) protein, a 15-kDa adipocyte protein previously sequenced in this laboratory from the corresponding cDNA.This publication has 41 references indexed in Scilit:
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