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۱Purification and Characterization of an Extracellular Poly–Galacturonase from Rhizoctonia solani Kühn (AG2–2)
نویسنده(ها):
اطلاعات انتشار: World Applied Sciences Journal، بيست و يكم،شماره۴، ۲۰۱۳، سال
تعداد صفحات: ۹
An extracellular poly–golacturonase (PG) (E.C. 3.2.1.15) was purified up to 116.77 fold from the culture filtrate of Rhizoctonia solani Kühn (AG2–2) by dialysis, precipitation with 0.7 saturation ammonium sulfate, gel filtration through Sephadex G–100 and ion–exchange chromatography on diethylaminoethyl cellulose with a yield of 72.397% and specific activity of 32.5 units\mgprotein. The purified enzyme exhibited maximal activity at pH 4.5 at 30° and was stable in the pH range of 3.0 to 5.0 and at temperature up to 30° k of the enzyme was m calculated to be 3.5 mg\ml. The molecular weight was determined by SDS–polyacrylamide gel electrophoresis to be 55 kDa. Participation of SH–groups in the catalytic sites of the enzyme is confirmed. Quantitative estimation of amino acids in the purified enzyme obtained from the culture of R. solani showed that it contained 17 amino acids and the proteins were rich with the aromatic amino acids, phenylalanine and tyrosine (50.59% of the total amino acids). And moderate amount of Acidic amino acids, aspartic and glutamic (23.78% of the total amino acids). And on the other hand, glycine is present in abstemious proportion (2.01% of the total amino acids).
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