Fractionation of human T lymphocytes on wheat germ agglutinin-sepharose

نویسندگان

  • U Hellström
  • M L Dillner
  • S Hammarström
  • P Perlmann
چکیده

T cells from human peripheral blood was purified by fractionation on columns charged with human immunoglobulin and rabbit anti-human immuno-globulin. When assayed with 125I- or fluorescein isothiocyanate-labeled wheat-germ agglutinin (WGA), a weakly binding and a strongly binding subpopulation could be distinguished. These T-cell subpopulations were fractionated on columns charged with WGA, convalently bound to Sepharose 6MB. The cells responding to the mitogens leukoagglutinin from Phaseolus vulgaris and concanavalin A were enriched in the strongly binding subpopulation (approximately 20% of the T cells) while they were depleted from the weakly binding subpopulation.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Interaction of sialoglycoproteins with wheat germ agglutinin-sepharose of varying ratio of lectin to Sepharose. Use for the purification of mucin glycoproteins from membrane extracts.

The influence of varying the amount of wheat germ agglutinin immobilized on Sepharose beads on the binding of glycoproteins to these beads was investigated. A series of wheat germ agglutinin-Sepharose gels containing between 0.10 and 10.0 mg of lectin/ml of gel was prepared, and the actual lectin content was established by acid hydrolysis of the gel followed by analysis of glycine, a major amin...

متن کامل

The interaction of wheat germ agglutinin with sialoglycoproteins. The role of sialic acid.

The role of sialic acid in the interaction of sialoglycoproteins with wheat germ agglutinin was investigated by using several well characterized saccharides and sialoglycoconjugates. N-Acetylneuraminic acid and neuramin 2 + 3 lactose, in addition to N-acetyl-Dglucosamine and its fil-+ 4 oligomers were found to be inhibitors of wheat germ agglutinin-induced hemagglutination. Neuraminic acid-/?-m...

متن کامل

The Interaction of Wheat Germ Agglutinin with Sialoglycoproteins

The role of sialic acid in the interaction of sialoglycoproteins with wheat germ agglutinin was investigated by using several well characterized saccharides and sialoglycoconjugates. N-Acetylneuraminic acid and neuramin 2 + 3 lactose, in addition to N-acetyl-Dglucosamine and its fil-+ 4 oligomers were found to be inhibitors of wheat germ agglutinin-induced hemagglutination. Neuraminic acid-/?-m...

متن کامل

Isolation of the Receptors for Wheat Germ Agglutinin and the Ricinus communis Lectins from Human Erythrocytes Using Affinity Chromatography*

of human erythrocyte ghosts were solubilized with 0.5yc Triton X-100 in 56 mM sodium borate, pH 8.0. This procedure solubilized 51% of the membrane protein, 81% of the sialic acid, 89% of the receptors for the Agaricus bisporus lectin and 70 to 75% of the wheat germ agglutinin and Ricinus communis lectin receptors. The solubilized glycoproteins were then separated by affinity chromatography on ...

متن کامل

Increase in cell surface wheat germ agglutinin binding in a rat hepatoma cell line dRLa 74 treated with concanavalin A.

Wheat germ agglutinin binding to a rat hepatoma cell line dRLa 74 treated with concanavalin A was studied. It increased depending on the concanavalin A concentration in the culture medium. The cells exhibited about twofold increase in wheat germ agglutinin-binding when pretreated with 50 micrograms/ml of concanavalin A for 48 h. The wheat germ agglutinin binding sites were shown to be localized...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:
  • The Journal of Experimental Medicine

دوره 144  شماره 

صفحات  -

تاریخ انتشار 1976