Purification and Properties of Codeinone Reductase (NADPH) from Papaver somniferum Cell Cultures and Differentiated Plants
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چکیده
منابع مشابه
extraction 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 ...
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The enzyme aldose (aldehyde) reductase was partially purified (142-fold) and characterized from Euonymus japonica leaves. The reductase, a dimer, had an average molecular weight of 67,000 as determined by gel filtration on Sephadex G-100. The enzyme was NADPH specific and reduced a broad range of substrates including aldoses, aliphatic aldehydes, and aromatic aldehydes. Maximum activity was obs...
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Salutaridine reductase (NADPH) is a key enzyme involves in morphine biosynthesis. BLASTP search waer performed to found orthologous proteins across different plant species. Domain analysis of all orthologous proteins was performed using Pfam and it was observed that Adh_short domain was conserved across all proteins. 3D structure of Salutaridine reductase was not available in PDB database, ther...
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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...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1995
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1995.132_1.x