Purification of Different Amphiphilic Forms of a Microvillus Aminopeptidase from Pig Small Intestine Using Immunoadsorbent Chromatography
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چکیده
منابع مشابه
Purification of endopeptidase-24.11 ('enkephalinase') from pig brain by immunoadsorbent chromatography.
Membrane preparations from striatum of pig brain contain endopeptidase activity towards iodoinsulin B-chain. Only 50% of the hydrolysis of insulin B-chain is inhibitable by phosphoramidon, and DEAE-cellulose chromatography can resolve the phosphoramidon-sensitive and -insensitive activities. The former activity (now designated 'endopeptidase-24.11') is responsible for hydrolysis of [D-Ala2,Leu5...
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Aminopeptidase A (aspartate aminopeptidase, EC 3.4.11.7) was purified 2000-fold from pig kidney cortex. The essential step in the purification was chromatography on an immunoadsorbent column prepared from a rabbit antiserum raised against pig intestinal aminopeptidase A. Glutamyl and aspartyl substrate were attacked most rapidly and their hydrolyses were stimulated by Ca2+. The 2-naphthylamide ...
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Sodium/D-glucose cotransport carriers solubilized from intestinal brush border membranes were purified and incorporated into liposomes made of soybean phospholipids, and transport properties of the reconstituted system were studied. The brush border membrane vesicles prepared from guinea pig small intestine were first treated with deoxycholate and papain in order to remove unnecessary membrane ...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1978
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1978.tb12476.x