Purification and properties of phloroglucinol reductase from Eubacterium oxidoreducens G-41
نویسندگان
چکیده
منابع مشابه
Purification and Properties of Phloroglucinol Reductase from
Phloroglucinol reductase was purified 90-fold to homogeneity from the anaerobic rumen organism Eubacterium oxidoreducem strain G-41. The enzyme is stable in the presence of air and is found in the soluble fraction after ultracentrifugation of cell extract. Ionexchange, hydrophobic interaction, and affinity chromatography were used to purify the enzyme. The native M, is 78,000, and the subunit M...
متن کاملextraction and acetylation of purified trypsin from bovin pancreas and study of some its physico-chemical properties
آنزیم تریپسین در شرایط قلیایی ناپایدار می باشد .و فعالیت پروتئولیتیکی تریپسین منجربه خود هضمی آن در جایگاههای خاصی می گردد. بنابر این آنزیمی با ناپایداری بالا محسوب میگردد. در سالهای اخیر موفق شدند که با ایجاد تغیرات شیمیایی با اضافه کردن فلزات خاص ، کلسیم و یا عمل استیلاسیون منجر به افزایش پایداری آنزیم تریپسین گردند. مطالعات در حال حاضر نشان می دهد که تریپسین استیله شده فعالیت آنزیمی خود را ...
15 صفحه اولPurification and properties of trimethylamine oxide reductase from Salmonella typhimurium.
The major inducible trimethylamine oxide reductase was purified from Salmonella typhimurium LT2. The molecular weights of the native enzyme were estimated to be 332,000 by gel filtration and 170,000 by nondenaturing disc gel electrophoresis. In sodium dodecyl sulfate-gel electrophoresis, the enzyme formed a single band of molecular weight 84,000. The isoelectric point was 4.28. Maximum activity...
متن کاملPurification and Properties of Nitrate Reductase from Escherichia coli KlZ*
The membrane-bound enzyme nitrate reductase from Escherichia coli has been solubilized and purified 112-fold. The purified enzyme appeared homogeneous by polyacrylamide gel electrophoresis and in the analytical ultracentrifuge. The molecular weight of the enzyme, as measured on an agarose column, was 720,000 and, as measured in the ultracentrifuge, was 773,600. The SO value was determined by se...
متن کاملPurification and properties of nitrite reductase from Escherichia coli K12.
NADH-nitrite oxidoreductase (EC 1.6.4) was purified to better than 95% homogeneity from batch cultures of Escherichia coli strain OR75Ch15, which is partially constitutive for nitrite reductase synthesis. Yields of purified enzyme were low, mainly because of a large loss of activity during chromatography on DEAE-cellulose. The quantitative separation of cytochrome c-552 from nitrite reductase 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: Journal of Biological Chemistry
سال: 1989
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)83759-0