Monocarboxamidomethyl Carbonic Anhydrase Purified by Affinity Chromatography
نویسندگان
چکیده
منابع مشابه
Monocarboxamidomethyl carbonic anhydrase purified by affinity chromatography.
A monocarboxamidomethyi derivative of human erythrocyte carbonic anhydrase B was purified by affinity chromatography. The modified enzyme possesses 3% of the COshydrating activity and 30% of the esterase activity of the native enzyme. The esterase activity is inhibited by the usual carbonic anhydrase inhibitors although the K; values are, in general, higher than for native enzyme. The pH depend...
متن کاملIsolation of Human Carbonic Anhydrase B and C and Apocarbonic Anhydrase by Affinity Chromatography
Human carbonic anhydrase B and C have been purified in high yields by affinity chromatography, using two different affinity gels, incorporating the potent benzenesulfonamide inhibitor, but coupled to Sepharose through different ,spacer-arms~. Although both affinity gels bind carbonic anhydrase B and C quantitatively, they exhibit different binding capacities. Sepharose-glycyi-L-tyrosine-azobenz...
متن کاملAn improved method for the purification of carbonic anhydrase isozymes by affinity chromatography.
Methods for purifying carbonic anhydrase (EC 4.2.1.1.) isozymes, carbonic anhydrase B (or I) and C (or IIL by affinity chromatography have been described by Falkbring et al. (1) and Whitney (2), in which affinity gels are formed by coupling, respectively, p-aminobenzenesulfonamide, and p-(aminomethyl)benzenesulfonamide to Sepharose polysaccharides by means of cyanogen bromide activation. Attemp...
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 کاملHuman placenta estrogen synthetase (aromatase) purified by affinity chromatography.
Microsomal estrogen synthetase (cytochrome P-450ES), also known as aromatase, was purified from fresh human placenta microsomes by DEAE-Trisacryl and testosterone-agarose chromatography. Estrogen synthetase assays were done with androstenedione as substrate, NADPH as electron donor, and a partially purified P-450 reductase from human placenta as the electron carrier. The specific cytochrome P-4...
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: Journal of Biological Chemistry
سال: 1973
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)44075-1