Properties of crystalline creatinine deiminase from Corynebacterium lilium.
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چکیده
منابع مشابه
Creatinine Deiminase Adsorption onto Silicalite-Modified pH-FET for Creation of New Creatinine-Sensitive Biosensor
In the work, silicalite particles were used for the surface modification of pH-sensitive field-effect transistors (pH-FETs) with the purpose of developing new creatinine-sensitive biosensor. Creatinine deiminase (CD) adsorbed on the surface of silicalite-coated pH-FET served as a bioselective membrane. The biosensor based on CD immobilized in glutaraldehyde vapor (GA) was taken as control. The ...
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 اولArginine deiminase from Halobacterium salinarium. Purification and properties.
Arginine deiminase from the extreme halophilic archaebacterium Halobacterium salinarium was purified to homogeneity in a four-step procedure with a 310-fold enrichment. The enzyme consists of two identical subunits of 55 kDa; its native molecular mass is 105 kDa. The pI of 4.7 indicates that acidic nature of the protein, which is evidenced by its amino acid composition, which shows an excess of...
متن کاملProperties of Crystalline Tryptophanase.
In 1903 Hopkins and Cole (1) identified tryptophan as the source of indole produced by bacterial cultures. The tryptophan-inducible enzyme responsible for this conversion, which is found most commonly in Escherichia coli, was subsequently named tryptophanase by Happold and Hoyle (2). Wood, Gunsalus, and Umbreit (3) showed that tryptophanase catalyzed the stoichiometric conversion of tryptophan ...
متن کاملCrystallization and properties of L-arginine deiminase of Pseudomonas putida.
Crystalline L-arginine deiminase of Pseudomonas putida was prepared by the following steps: sonic disruption, ammonium sulfate fractionation, protamine sulfate treatment, DEAE-cellulose column chromatography, and L-arginine-Sepharose 6B chromatography followed by crystallization. This procedure yields a crystalline pure enzyme with a 45% recovery of the activity in crude cell-free extracts. The...
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ژورنال
عنوان ژورنال: Agricultural and Biological Chemistry
سال: 1980
ISSN: 0002-1369,1881-1280
DOI: 10.1271/bbb1961.44.1787