埃德曼退化
肽序列
生物化学
跨膜结构域
氨基酸
信号肽
生物
跨膜蛋白
信使核糖核酸
细胞质
分子生物学
化学
基因
受体
作者
Mike Mueckler,Carla Caruso,S. A. Baldwin,Maria Panico,I Blench,HR Morris,W. Jeffrey Allard,G E Lienhard,Lodish Hf
出处
期刊:Science
[American Association for the Advancement of Science (AAAS)]
日期:1985-09-06
卷期号:229 (4717): 941-945
被引量:1482
标识
DOI:10.1126/science.3839598
摘要
The amino acid sequence of the glucose transport protein from human HepG2 hepatoma cells was deduced from analysis of a complementary DNA clone. Structural analysis of the purified human erythrocyte glucose transporter by fast atom bombardment mapping and gas phase Edman degradation confirmed the identity of the clone and demonstrated that the HepG2 and erythrocyte transporters are highly homologous and may be identical. The protein lacks a cleavable amino-terminal signal sequence. Analysis of the primary structure suggests the presence of 12 membrane-spanning domains. Several of these may form amphipathic alpha helices and contain abundant hydroxyl and amide side chains that could participate in glucose binding or line a transmembrane pore through which the sugar moves. The amino terminus, carboxyl terminus, and a highly hydrophilic domain in the center of the protein are all predicted to lie on the cytoplasmic face. Messenger RNA species homologous to HepG2 glucose transporter messenger RNA were detected in K562 leukemic cells, HT29 colon adenocarcinoma cells, and human kidney tissue.
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