Glucose-6-phosphate dehydrogenase. Purification and partial characterization.
نویسندگان
چکیده
منابع مشابه
Glucose-6-phosphate Dehydrogenase PURIFICATION AND PARTIAL CHARACTERIZATION
Glucose-6-phosphate dehydrogenase has been purified lOOO-fold from pig liver. This enzyme exists as an active dimer of molecular weight 133,000 and an inactive monomer of molecular weight 67,500. The pH of maximum activity is 8.5 and the ionic strength maximum is 0.1 to 0.5 M. Glucose-6-phosphate dehydrogenase is highly specific for NADP+ and glucose B-phosphate. Apparent K, values of 3.6 pM an...
متن کاملGalactose-6-phosphate dehydrogenase. Purification and partial characterization.
A new enzyme, galactose-6-phosphate dehydrogenase has been purified about 50-fold from goat liver. The enzyme can be distinguished from the nonspecific hexose-6-phosphate dehydrogenase and glucose-6-phosphate dehydrogenase by its high substrate specificity and absolute pyridine nucleotide requirement. In contrast to the hexose-6-phosphate dehydrogenase, this enzyme is located exclusively in the...
متن کاملGlucose-6-Phosphate Dehydrogenase Deficiency and Neonatal Hyperbilirubinemia
Background: Jaundice is affecting over 60-80 percent of neonates in the first week of life. Glucose-6-phosphate dehydrogenase (G6PD) deficiency, which is an important cause of pathologic hyperbilirubinemia, can lead to hemolytic anemia, jaundice and kernicterus. The present study was performed to determine the prevalence of G6PD deficiency among icteric neonates in Shirvan, Iran. Methods: This...
متن کاملPurification and properties of Penicillium glucose 6-phosphate dehydrogenase.
1. Glucose 6-phosphate dehydrogenase was isolated and partially purified from a thermophilic fungus, Penicillium duponti, and a mesophilic fungus, Penicillium notatum. 2. The molecular weight of the P. duponti enzyme was found to be 120000+/-10000 by gelfiltration and sucrose-density-gradient-centrifugation techniques. No NADP(+)- or glucose 6-phosphate-induced change in molecular weight could ...
متن کاملPurification and properties of d-glucose-6-phosphate dehydrogenase.
n-Glucose-6-phosphate dehydrogenase (Zwischenferment) was discovered by Warburg and Christian in 1931 (1, 2). An active preparation was obtained then from horse erythrocytes and in 1932 from the Lebedev juice made from brewers’ yeast (3). Because of its extreme specificity, this enzyme has become an important analytical tool. Various preparations of it have been described, the first being those...
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: 1976
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(17)33580-9