| Literature DB >> 3029095 |
L Rönnstrand, M P Beckmann, B Faulders, A Ostman, B Ek, C H Heldin.
Abstract
The receptor for platelet-derived growth factor has been purified to homogeneity on a large scale from porcine uterus. The purification procedure utilizes solubilization of uterus membranes by Triton X-100, followed by sequential chromatographies on wheat germ agglutinin-Sepharose, fast protein liquid chromatography Mono-Q, and anti-phosphotyrosine-Sepharose. About 160 micrograms of homogeneous and functionally active 170-kDa receptor could be purified from 5 kg of uterus tissue. The pure receptor responded to platelet-derived growth factor stimulation by autophosphorylation, indicating that the receptor has a kinase domain as an integral part of the molecule. A rabbit antiserum was produced against the pure receptor, which specifically recognizes the intact 170-kDa receptor.Entities:
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Year: 1987 PMID: 3029095
Source DB: PubMed Journal: J Biol Chem ISSN: 0021-9258 Impact factor: 5.157