Affinity Chromatography of Tryptophan Synthase fromEscherichia coli
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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...
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We have synthesized bromoacetylpyridoxamine phosphate and bromoacetylpyridoxamine and have shown that they meet three criteria for affinity labels of the beta2 subunit of tryptophan synthase: (i) the kinetic data of inactivation indicate that a binary complex is formed prior to covalent attachment; (ii) inactivation is largely prevented by the presence of pyridoxal phosphate; and (iii) inactiva...
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 کاملAffinity Chromatography of Lectins
Affinity chromatography is a technique used to purify compounds, such as proteins, that have the ability to non-covalently and reversibly bind specific molecules, known as ligands. This method differs from the classical chromatography techniques in that the protein is purified on the basis of a unique biochemical property. In affinity chromatography, the ligand is covalently attached to a matri...
متن کاملProduction of a novel tryptophan analog, beta-1-indazole-L-alanine with tryptophan synthase of Escherichia coli.
The tryptophan synthase alpha 2 beta 2 complex from Escherichia coli has been found to catalyze the beta-replacement reaction of L-serine with indazole, an indole analog which has a nitrogen atom at the 2-position (pyrazole ring). The reaction product was isolated and identified as beta-indazolealanine by mass spectrometric, elemental and NMR analyses. Careful assignment of 1H- and 13C-signals ...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1979
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1979.tb13052.x