SIMPLIFIED TECHNIQUE TO ISOLATE THE PORCINE AND HUMAN ILEAL INTRINSIC-FACTOR RECEPTORS AND STUDIES ON THEIR SUBUNIT STRUCTURES

被引：34

作者：

KOUVONEN, I

GRASBECK, R

机构：

[1] Minerva Foundation Institute for Medical Research, 00101 Helsinki

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1979年 / 86卷 / 02期

关键词：

D O I：

10.1016/0006-291X(79)90873-8

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The porcine intestinal intrinsic factor receptor was isolated with affinity chromatography utilizing vitamin B12-intrinsic factor-Sepharose and pH adjustments. The purification was about 70 000-fold and in sodium dodecyl sulphate electrophoresis it resolved into two carbohydrate-containing 70 000 and 130 000 dalton bands (alpha and beta subunits) indicating purity. The human receptor was similarly purified and radioiodinated for further studies. It was also composed of two subunits (90 000 and 140 000 dalton). The alpha subunits bound to anti-intrinsic factor antisera. © 1979.

引用

页码：358 / 364

页数：7

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