Isolation of a nicotine binding site from rat brain by affinity chromatography.
نویسندگان
چکیده
منابع مشابه
A Cytokinin-binding Protein from Wheat Germ: Isolation by Affinity Chromatography and Properties.
A cytokinin-binding protein has been isolated from wheat germ via ammonium sulfate precipitation, carboxymethyl Sephadex chromatography, and affinity chromatography on a column substituted with a derivative of kinetin riboside. On Sephadex G-200, the protein migrated with an apparent molecular weight of 122,000 daltons. The dissociation constant for kinetin was determined by equilibrium dialysi...
متن کاملPreparation of Plasminogen by Affinity Chromatography
Background: Plasminogen is one of the compounds derived from human plasma. Activation of plasminogen produces plasmin. Plasmin is able to lyse fibrinogen, fibrin, and some other human plasma proteins. The aim of the present work was to study the separation of human plasminogen by affinity chromatography using gel lysine Sepharose. Materials and Methods: Normal human plasma was used as the...
متن کاملThe isolation of rhodanese from Pseudomonas aeruginosa by affinity chromatography.
Rhodanese (thiosulphate : cyanide sulphur-transferase; EC 2 . 8 . I . I) was originally ,described by Lang (1933). The enzyme catalyses the formation of thiocyanate from cyanide and thiosulphate according to the reaction : S20!+ CN-+ SCN+ SO:-. Rhodanese activity has been demonstrated in most mammalian tissues, with the greatest activity present in liver and kidney. The enzyme has been purified...
متن کاملIsolation of trypsins by affinity chromatography.
To learn the molecular mechanism of an enzyme action, first the protein has to be purified. Because of its simplicity and reproducibility, affinity chromatography has become a adopted method throughout the scientific community. Affinity chromatography occupies a unique place in separation technology since it is the only technique which enables purification of almost any biomolecules on the basi...
متن کاملIsolation by covalent affinity chromatography of the penicillin-binding components from membranes of Bacillus subtilis.
An affinity chromatography technique was developed to isolate the five penicillin-binding components present in Bacillus subtilis membranes. The proteins were solubilized by the detergent Nonidet P-40, bound covalently to penicillin-substituted Sepharose, and subsequently eluted from the matrix with neutral hydroxylamine, which cleaves the penicilloyl-enzyme bond. Penicillin binding-component V...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 1983
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.80.11.3536