The 56-59-kilodalton protein identified in untransformed steroid receptor complexes is a unique protein that exists in cytosol in a complex with both the 70- and 90-kilodalton heat shock proteins
作者： Edwin R. Sanchez , Lee E. Faber , William J. Henzel , William B. Pratt
DOI: 10.1021/BI00473A021
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摘要: It has previously been shown that 9S, untransformed progestin, estrogen, androgen, and glucocorticoid receptor complexes in rabbit uterine liver cytosols contain a 59-kDa protein [Tai, P. K., Maeda, Y., Nakao, Wakim, N. G., Duhring, J. L., & Faber, L. E. (1986) Biochemistry 25, 5269-5275]. In this work we show the monoclonal antibody KN 382/EC1 raised against reacts with cytosol prepared from human IM-9 lymphocytes but not 4S salt-transformed receptors. The recognized by EC1 is 56-kDa (p56) of moderate abundance located predominantly cytoplasm indirect immunofluorescence. There are at least six isomorphs p56 two-dimensional gel analysis. N-Terminal sequencing (20 amino acids) shows unique protein. When immunoadsorbed cell cytosol, both 70- 90-kDa heat shock proteins coadsorbed an immune-specific manner. Neither directly antibody. We conclude exists higher order complex containing hsp70 hsp90, which turn have found to be associated steroid
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