SOLUBILIZATION AND PARTIAL CHARACTERIZATION OF A PHYTOHEMAGGLUTININ RECEPTOR SITE FROM HUMAN ERYTHROCYTES
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چکیده
منابع مشابه
Solubilization and partial characterization of a phytohemagglutinin receptor site from human erythrocytes.
Trypsin treatment of human erythrocytes releases a soluble glycopeptide which binds to phytohemagglutinin and abolishes the erythroagglutinating and lymphocyte-stimulating properties of this molecule. The glycopeptide has been purified by alkaline borohydride treatment, proteolytic digestion, gel filtration, and DEAE-cellulose chromatography. The most highly purified glycopeptide has a molecula...
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A highly purified glycopeptide with potent phytohemagglutinin (PHA) receptor site activity has been isolated from human erythrocyte membranes. The glycopeptide was released from the membranes by trypsin, treated with alkaline borohydride, and purified by repeated gel filtration, further proteolytic digestion with Pronase, and diethylaminoethyl cellulose chromatography. It has a molecular weight...
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Human erythrocyte transketolase (sedoheptulose-7-phosphate: D-glyceraldehyde-3-phosphate, glycolaldehyde transferase, E.C. 2.2.1.1.) has been isolated from erythrocytes with a specific activity of 59.84 U/mg. SDS-PAGE and SE-HPLC were used both as a measure of purity and as a preparative mean to obtain a higher degree of purity. Four protein bands corresponding to molecular weights of 32,0...
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 1969
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.63.4.1439