Purification and properties of nuclease gamma from Ustilago maydis.
نویسندگان
چکیده
منابع مشابه
Purification and characterization of aminopeptidase (pumAPE) from Ustilago maydis.
The aminopeptidase pumAPE was purified from the haploid fungus Ustilago maydis FB1 strain. The purification procedure consisted of ammonium sulfate fractionation and three chromatographic steps, which included anion-exchange, hydrophobic interaction, and gel filtration chromatography, resulting in a 23% recovery. The molecular mass of the dimeric enzyme was estimated to be 110 kDa and 58 kDa by...
متن کاملسیتولوژی Ustilago maydis
رفتار هسته در تلیوسپور، بازیدیوسپور و میسلیومهای Ustilago maydis مورد بررسی قرار گرفت. جهت کشت تلیوسپورها از محیط PDA + 10% دکستروز استفاده گردید. مطالعه رفتار هسته با استفاده از میکروسکوپ اپیفلورسنت و رنگآمیزی با دو رنگ اتیدیوم برماید و اکردین اورنج صورت پذیرفت. هسته در تلیوسپور کروی و بزرگ و اکثر فضای داخلی آن را اشغال نموده است. بازیدیوسپورها (اسپوریدیوم) به صورت غیرانگلی و به روش جوانهز...
متن کاملGlycolysis in Ustilago maydis.
The kinetic parameters of the 10 glycolytic enzymes and glycolytic fluxes were determined for the first time in Ustilago maydis. Enzyme activities in yeast grown in minimal medium and harvested in the stationary stage were twofold higher than those from yeast grown in rich medium. In contrast, in yeast harvested in the exponential stage, the enzyme activities were higher in cells grown in rich ...
متن کاملUstilago maydis as a Pathogen.
The Ustilago maydis-maize pathosystem has emerged as the current model for plant pathogenic basidiomycetes and as one of the few models for a true biotrophic interaction that persists throughout fungal development inside the host plant. This is based on the highly advanced genetic system for both the pathogen and its host, the ability to propagate U. maydis in axenic culture, and its unique cap...
متن کاملPartial purification and properties of a nuclease from chicken pancreas.
A nuclease has been isolated from an acid homogenate of chicken pancreas and purified over 300-fold. The purified preparation was free of phosphomonoesterase and phosphodiesterase activity, but rapidly hydrolyzed ribonucleic acid and deoxyribonucleic acid. The enzyme which by several criteria was a single protein required Mg++ or Mn++ for activity; addition of excess ethylenediaminetetraacetate...
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: 1984
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(17)43253-4