نتایج جستجو برای: sephadex chromatography

تعداد نتایج: 108287  

Journal: :The Journal of biological chemistry 1983
J F Grippo W Tienrungroj M K Dahmer P R Housley W B Pratt

Extraction of rat liver cytosol with 10% charcoal at 4 degrees C inactivates specific glucocorticoid-binding capacity. The steroid-binding capacity of extracted cytosol can be restored by adding dithiothreitol or by incubating with boiled liver cytosol at 20 degrees C in the presence of 10 mM sodium molybdate. Two components of boiled cytosol are required for receptor activation: NADPH and an e...

Journal: :The Journal of biological chemistry 1971
J M Prescott S H Wilkes F W Wagner K J Wilson

The extracellular aminopeptidase of Aeromonas proteofytica was purified to homogeneity by a simplified procedure that proved feasible for the isolation of gram quantities of this enzyme. Precipitation with ammonium sulfate and acetone, heating at 70”, and chromatography on Sephadex G-75 and DEAE-Sephadex yielded a product that showed a high degree of purity by polyacrylamide and free boundary e...

Journal: :The Journal of biological chemistry 1974
N E Engström A Holmgren A Larsson S Söderhäll

The reduced form of thioredoxin, a low molecular weight hydrogen transport protein, was isolated from calf liver. The purification involved heat treatment and chromatography on DEAE-cellulose, Sephadex G-SO, and CM-cellulose, and it resulted in an apparently pure protein after a 4,000-fold purification with a final yield of 30%. The thioredoxin preparation obtained was homogeneous as judged by ...

2011
P. Dineshkumar

The enzyme L-Amino Acid Oxidase (LAAO) is widely distributed in snake venoms, contributes a reasonable toxicity to the venoms. However LAAO from Indian cobra (Naja naja ) snake venom has not yet isolated previously. In the present study LAAO from Indian cobra (Naja naja ) snake venom was purified by sequential steps of cation exchange chromatography (CM-Sephadex C-25; CM-52 cellulose), followed...

Journal: :Hypertension 1980
K Morimoto M Matsunaga A Hara C Kawai

The mechanism of activation of inactive renin was studied in normal human plasma. The molecular weight of active renin and those of inactive renin before and after activation were analyzed by sephadex gel filtration. Active renin of human plasma had a molecular weight of 48,000 +/- 1000. Trypsin treatment and cold treatment activated inactive renin of a molecular weight of 54,000 +/- 1000. The ...

Journal: :The Biochemical journal 1980
K Muniyappa P R Adiga

A high-affinity riboflavin -binding protein was isolated and characterized for the first time from pregnant-rat sera by affinity chromatography on a lumiflavin-agarose column. The purified protein was homogeneous by the criteria of analytical polyacrylamide-gel disc electrophoresis, gel-filtration chromatography on Sephadex G-100 and sodium dodecyl sulphate/polyacrylamide-gel electrophoresis. I...

Journal: :Applied and environmental microbiology 1989
B J Taller T Y Wong

Azotobacter vinelandii OP was grown to stationary phase in defined medium. The cell-free culture medium was analyzed for cytokinin content by XAD-2 and Sephadex LH-20 chromatography, thin-layer chromatography, tobacco callus bioassay, and enzyme immunoassay. Three cytokinin-active fractions were detected and tentatively identified as trans-zeatin, isopentenyladenosine, and isopentenyladenine. T...

Journal: :The Journal of antibiotics 2001
R Uchida H Tomoda M Arai S Omura

Chlorogentisylquinone, a new inhibitor of neutral sphingomyelinase activity, was purified from the culture broth of a fungal strain FOM-8108 isolated from a marine environment by solvent extraction, silica gel chromatography and Sephadex LH-20 chromatography. Its chemical structure was elucidated by spectroscopic studies including 1H, 13C, DEPT, HMQC and HMBC NMR experiments. Chlorogentisylquin...

Journal: :journal of sciences islamic republic of iran 0

the first enzyme of the pathway for uridine diphosphate n-acetyl-d-glucosamine (udpag) biosynthesis i.e. l-glutamine: d-fructose 6-p amidotransferase (e.c. 2.6.1.16) was purified 52-fold from human placenta using methanol fractionation and column chromatography on deae-sephadex a-50. the enzyme showed optimal activity in a broad range of ph from 5.8 to 7.8 in both phosphate and cacodylate buffe...

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