Chromatographic resolution of insulin receptor from insulin-sensitive D-glucose transporter of adipocyte plasma membranes.
Chromatographic resolution of insulin receptor from insulin-sensitive D-glucose transporter of adipocyte plasma membranes.
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脂肪细胞质膜胰岛素敏感 D-葡萄糖转运蛋白的胰岛素受体的色谱分离。
DOI:
10.1021/bi00504a036
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发表时间:
1981
期刊:
影响因子:
2.9
通讯作者:
Czech,MP
中科院分区:
文献类型:
--
作者:
Carter-Su,C;Pilch,PF;Czech,MP
Christin Carter-Su,* Paul F. Pilch, and Michael P. Czech abstract: The chromatographic properties of the affinity-labeled adipocyte insulin receptor and the insulin-sensitive hexose transporter were evaluated in order to test the hypothesis that the transportermight be composed of receptor polypeptides.[I25I] Insulin was linked specifically and cova-lently to the high-affinity insulinreceptor in dimethylmaleic anhydride extracted rat adipocyte plasma membranes by using the cross-linking reagent disuccinimidyl suberate [Pilch, P. F., & Czech, M. P.(1979) J. Biol. Chem. 254, 3375-3381], The membranes were solubilized with sodium cholate and resolved into three peaks of protein following hydroxylapatite chro-matography. The first or void volume peak contained 10-20% of the protein, no receptor-bound [125I] insulin, and no cytochalasin B sensitive D-glucose transport activity when recon-stituted into phospholipid vesicles. The second major peak contained about half of the protein and as much as 87% of the affinity-labeled receptor but no hexose transport activity. The third peak contained 30-40% of the protein, 13-20% of-A-lthough significant advances have been made in understanding how hormones interact with receptor proteins and what changes in cell function are brought about as a result of hormone-receptorinteractions, little is known about the spatial relationship of membrane-bound hormone receptors and their effector systems. Two of the hormone receptoreffector systems for which such information is available are the acetylcholine and/3-adrenergic receptor-effector systems. Huganir et al.(1979) have recently reported that the ace-tylcholine-dependent Na+ channel appears to be part of the same protein complex as the acetylcholine receptor. The
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DOI:
10.1016/s0021-9258(17)33476-2
发表时间:
1976
期刊:
The Journal of biological chemistry
影响因子:
--
作者:
M. Czech
通讯作者:
M. Czech
DOI:
10.1016/s0021-9258(19)45480-x
发表时间:
1972
期刊:
The Journal of biological chemistry
影响因子:
--
作者:
P. Cuatrecasas
通讯作者:
P. Cuatrecasas
DOI:
--
发表时间:
1980
影响因子:
11.1
作者:
L. Limbird;D. Gill;R. Lefkowitz
通讯作者:
R. Lefkowitz
DOI:
10.1016/s0021-9258(17)39993-3
发表时间:
1977
期刊:
The Journal of biological chemistry
影响因子:
--
作者:
M. F. Shanahan;M. Czech
通讯作者:
M. Czech
DOI:
10.1073/pnas.74.9.3710
发表时间:
1977
影响因子:
11.1
作者:
G. Vauquelin;P. Geynet;J. Hanoune;A. Strosberg
通讯作者:
A. Strosberg