COMPARATIVE-ANALYSIS OF THE GAP JUNCTION PROTEIN FROM RAT-HEART AND LIVER - IS THERE A TISSUE-SPECIFICITY OF GAP-JUNCTIONS
COMPARATIVE-ANALYSIS OF THE GAP JUNCTION PROTEIN FROM RAT-HEART AND LIVER - IS THERE A TISSUE-SPECIFICITY OF GAP-JUNCTIONS
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DOI：
10.1016/0092-8674(83)90188-5
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发表时间：
1983-01-01
期刊：
影响因子：
64.5
通讯作者：
REVEL, JP
中科院分区：
文献类型：
--
作者：
GROS, DB;NICHOLSON, BJ;REVEL, JP
从大鼠心脏和肝脏分离间隙连接，这些组织中的连接在外观和生理学上是典型的。通过EM（薄切片和负染色）和十二烷基硫酸钠-聚丙烯酰胺凝胶电泳（SDS-PAGE）监测所获得的级分的纯度。心肌间隙连接由MW 28，000的单一多肽组成，显然衍生自MW 30，000的蛋白质。肝脏间隙连接也由MW 28，000的单一天然蛋白质组成，如先前报道的。胰蛋白酶对分离的连接进行彻底消化，类似地切割这两种蛋白质，同时保持其特征性连接晶格结构完整。然而，通过胰蛋白酶和α-胰蛋白酶的二维肽图谱比较心脏和肝脏连接蛋白是不可能的。胰凝乳蛋白酶片段，然后进行高压液相色谱，揭示这些蛋白质之间没有同源性。
Gap junctions were isolated from both rat heart and liver, tissues where junctions are typical in appearance and physiology. The purity of the fractions obtained was monitored by EM (thin-sectioning and negative staining) and sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). The myocardial gap junctions are comprised of a single polypeptide of MW 28,000, apparently derived from a protein of MW 30,000. Hepatic gap junctions are also comprised of a single native protein of MW 28,000 as previously reported. Exhaustive trypsin digestion of the isolated junctions cleaves both of these proteins similarly, while leaving their characteristic junctional lattice structures intact. However, comparison of heart and liver junctional proteins by 2-dimensional peptide mapping of tryptic and .alpha.-chymotryptic fragments, followed by high pressure liquid chromatography, reveals no homology between these proteins.