Purification and properties of 5,10-methenyltetrahydromethanopterin cyclohydrolase from Methanosarcina barkeri
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چکیده
منابع مشابه
Purification and properties of the 5,10-methenyltetrahydromethanopterin cyclohydrolase from Methanobacterium thermoautotrophicum.
The 5,10-methenyltetrahydromethanopterin cyclohydrolase of Methanobacterium thermoautotrophicum was purified 128-fold to homogeneity. The enzyme had a subunit Mr of 41,000 as indicated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. From high-performance size exclusion chromatography of the native protein, an Mr of 82,000 was determined, suggesting a dimer of identical subunits. T...
متن کاملPurification and properties of 5,10-methenyltetrahydrofolate cyclohydrolase from Clostridium formicoaceticum.
Methenyltetrahydrofolate cyclohydrolase (EC 3.5.4.9) from Clostridium formicoaceticum has been purified to a specific activity of 469 mumol min-1 mg-1 at 35 degrees C, pH 7.2. The purified enzyme is homogeneous as judged by polyacrylamide disc gel electrophoresis, sedimentation velocity, and gel filtration profiles. The molecular weight is 41,000 +/- 200 as determined by sedimentation equilibri...
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Methane formation from acetate by resting cells of Methanosarcina barkeri was accompanied by an increase in the intracellular ATP content from 0.9 to 4.0 nmol/mg of protein. Correspondingly, the proton motive force increased to a steady-state level of -120 mV. The transmembrane pH gradient however, was reversed under these conditions and amounted to +20 mV. The addition of the protonophore 3,5,...
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Carbon monoxide dehydrogenase from Methanosarcina barkeri, purified to 95% homogeneity, contains 30 Fe, 2 Ni, 1 Zn, and 1 Cu (per alpha 2 beta 2 enzyme). Core extrusion experiments indicate 6 [4Fe-4S] clusters/tetramer, and electron paramagnetic resonance (epr) spectroscopy detects at least one of these clusters, in the reduced form, with apparent g values of 2.05, 1.94, and 1.90, and Em9.2-390...
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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 ...
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ژورنال
عنوان ژورنال: Journal of Bacteriology
سال: 1990
ISSN: 0021-9193,1098-5530
DOI: 10.1128/jb.172.2.564-571.1990