Partial Purification and Characterization of d-Ribose-5-phosphate Reductase from Adonis vernalis L. Leaves
نویسندگان
چکیده
منابع مشابه
Partial Purification and Characterization of d-Ribose-5-phosphate Reductase from Adonis vernalis L. Leaves.
This study presents evidence for a new enzyme, d-ribose-5-P reductase, which catalyzes the reaction: d-ribose-5-P + NADPH + H(+) --> d-ribitol-5-P + NADP(+). The enzyme was isolated from Adonis vernalis L. leaves in 38% yield and was purified 71-fold. The reductase was NADPH specific and had a pH optimum in the range of 5.5 to 6.0. The Michaelis constant value for d-ribose-5-P reduction was 1.3...
متن کاملCharacterization and Partial Purification of Aldose-6-phosphate Reductase (Alditol-6-Phosphate:NADP 1-Oxidoreductase) from Apple Leaves.
Aldose-6-phosphate reductase (alditol 6-phosphate:NADP 1-oxidoreductase) was isolated and characterized from mature apple leaves (Malus domestica cv. Starkrimson). The enzyme was purified 79-fold. The enzyme catalyzed the following reversible reaction: d-glucose 6-phosphate + NADPH + H(+) right arrow over left arrow d-sorbitol 6-phosphate + NADP(+). No activity was detected when NAD(+) was subs...
متن کاملPARTIAL PURIFICATION AND CHARACTERIZATION OF B-GALACTOSIDASE FROM ASPERGILLUS NIGER UV-5
The enzyme pgalactosidase from a mutant strain of A. niger UV-5 was partially purified using ammonium sulfate and acetone. The saturation range of 60-80% ammonium sulfate was found to yield 60.5% enzyme recovery with 2.4 fold purification. Acetone precipitation at enzyme: acetone ratio of 1 : 1.5 brought about a higher yield i.e. 68% and three-fold purification. The combined procedures of ...
متن کاملD-ribose-5-phosphate isomerase from spinach: heterologous overexpression, purification, characterization, and site-directed mutagenesis of the recombinant enzyme.
A cDNA encoding spinach chloroplastic ribose-5-phosphate isomerase (RPI) was cloned and overexpressed in Escherichia coli, and a purification scheme for the recombinant enzyme was developed. The purified recombinant RPI is a homodimer of 25-kDa subunits and shows kinetic properties similar to those of the homodimeric enzyme isolated from spinach leaves (A. C. Rutner, 1970, Biochemistry 9, 178-1...
متن کاملPartial purification and characterization of endoproteinases from senescing barley leaves.
Two major endoproteinases were purified from senescing primary barley leaves. The major enzyme (EP(1)) appeared to be a thiol proteinase and accounted for about 85% of the total proteolytic activity measured in vitro. This proteinase was purified 5,800-fold and had a molecular weight of 28,300. It was highly unstable in the absence of dithiothreitol or at a pH greater than 7.5. Leupeptin, at a ...
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: Plant Physiology
سال: 1985
ISSN: 0032-0889,1532-2548
DOI: 10.1104/pp.78.4.758