Garnett D, Spruyt L L, Beyers A D
Department of Medical Biochemistry, University of Stellenbosch, Tygerberg, South Africa.
Braz J Med Biol Res. 1994 Feb;27(2):269-73.
We have previously demonstrated the non-covalent association of the protein tyrosine kinases p56lck and p60fyn together with a number of substrates for phosphorylation with rat thymocyte Thy-1. Here we present evidence that one of these associated phosphoproteins, p85, is associated by disulphide bridging with another polypeptide, demonstrating that it is an integral membrane protein with an extracellular domain. We also show that phosphatidylinositol 3 kinase activity may be coprecipitated with Thy-1 in Brij 96 thymocyte lysates.
我们之前已经证明,蛋白酪氨酸激酶p56lck和p60fyn与一些用于大鼠胸腺细胞Thy-1磷酸化的底物存在非共价结合。在此我们提供证据表明,这些相关的磷蛋白之一p85通过二硫键与另一种多肽相连,这表明它是一种具有细胞外结构域的整合膜蛋白。我们还表明,磷脂酰肌醇3激酶活性可能在Brij 96胸腺细胞裂解物中与Thy-1共沉淀。