Purification by affinity chromatography of thermostable glyceraldehyde 3-phosphate dehydrogenase from Thermus aquaticus
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چکیده
منابع مشابه
Purification by affinity chromatography of thermostable glyceraldehyde 3-phosphate dehydrogenase from Thermus aquaticus.
activities of the key enzymes of gluconeogenesis in the liver and kidney of the foetal guinea pig have been followed. The foetal guinea pigs used had a gestational age of 68-72 days. Pyruvate carboxylase was present at very low activities in the kidney of the foetus and neonatal animal and also in the foetal liver until day 50, when it increased in activity to reach a value by day 60 of more th...
متن کاملThermostable aldolase from Thermus aquaticus.
Data are presented on the purification and properties of the thermostable fructose-1,6-diphosphate aldolase of Thermus aquaticus, a nonsporulating, extreme thermophile. The enzyme shows little activity at temperatures below 60 C and optimal activity at about 95 C. The enzyme was purified 43-fold by diethylaminoethyl cellulose column chromatography and Sephadex G-200 gel filtration. The enzyme i...
متن کاملSingle Step Purification of Novel Thermostable and Chelator Resistant Amylase from Bacillus Licheniformis RM44 by Affinity Chromatography
Bacillus licheniformis RM44 was isolated from hot spring near Karachi and screened forthe production of extracellular amylase Amy RM44. Amy RM44 was purified to homogeneityon a single step by affinity chromatography using insoluble corn starch. The molecular weightof Amy RM44 was estimated to be 66 kDa by SDS–PAGE and zymographic analysis. Nine foldpurification was achieved with the specific ac...
متن کاملSingle Step Purification of Novel Thermostable and Chelator Resistant Amylase from Bacillus Licheniformis RM44 by Affinity Chromatography
Bacillus licheniformis RM44 was isolated from hot spring near Karachi and screened forthe production of extracellular amylase Amy RM44. Amy RM44 was purified to homogeneityon a single step by affinity chromatography using insoluble corn starch. The molecular weightof Amy RM44 was estimated to be 66 kDa by SDS–PAGE and zymographic analysis. Nine foldpurification was achieved with the specific ac...
متن کاملMechanism of glyceraldehyde-3-phosphate transfer from aldolase to glyceraldehyde-3-phosphate dehydrogenase.
The catalytic interaction of glyceraldehyde-3-phosphate dehydrogenase with glyceraldehyde 3-phosphate has been examined by transient-state kinetic methods. The results confirm previous reports that the apparent Km for oxidative phosphorylation of glyceraldehyde 3-phosphate decreases at least 50-fold when the substrate is generated in a coupled reaction system through the action of aldolase on f...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1972
ISSN: 0306-3283
DOI: 10.1042/bj1300024p