Purifying of phytohormone by immuno affinity chromatography.
نویسندگان
چکیده
منابع مشابه
Preparation 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 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 start...
متن کاملThe purification by immuno-affinity chromatography of bacterial methionyl-(human somatotropin)
kallikrein activities (Fig. 2a). a,-Proteinase inhibitor concentrations (0.28, 4.44 and 4.44mg/ml) were chosen that produced inhibition (to 37,42 and 32% of control rates respectively) of thrombin(substrate S-2238), 7s-NGF(substrate s-2302) and kallikrein(substrate s-2302) catalysed amidolysis respectively. Heparin alleviated a,-proteinase inhibition of thrombin, but did not affect inhibition o...
متن کاملPurification by Affinity Chromatography
The glycine receptor of rat spinal cord was solubilized with the nonionic detergent Triton X-100 and subsequently purified by affinity chromatography on aminostrychnine-agarose and wheat germ agglutininSepharose. An overall purification of 1950-fold was achieved. Polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate and mercaptoethano1 revealed three glycine receptor-asso...
متن کاملProtein Purification by Affinity Chromatography
The preparation of a number of agarose and polyacrylamide bead derivatives useful in the purification of proteins by afhnity chromatography is described. These techniques permit (a) the attachment of ligands to the gel through extended hydrocarbon chains which place the ligand at varying distances from the gel matrix backbone; (b) the covalent attachment of ligands to agarose or polyacrylamide ...
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ژورنال
عنوان ژورنال: Kagaku To Seibutsu
سال: 1991
ISSN: 0453-073X,1883-6852
DOI: 10.1271/kagakutoseibutsu1962.29.270