نتایج جستجو برای: gel chromatography

تعداد نتایج: 195952  

2003
A. Zdrojewski

Plasma/serum protein patterns in human fetuses and infants: a study by high-resolution two-dimensional polyacrylamide gel electrophoresis. Applied and Theoretical Electrophoresis 3: 183}190. Tissot JD and Spertini F (1995) Analysis of immunoglobulins by two-dimensional gel electrophoresis. Journal of Chromatography A 698: 225}250. Tissot JD, Invernizzi F, Schifferli J, Spertini F and Schneider ...

Journal: :Journal of biochemistry and molecular biology 2005
Hee-Joong Park Hyun-Young Cho Kwang-Hoon Kong

A glutathione S-transferase (GST) from Lactuca sativa was purified to electrophoretic homogeneity approximately 403-fold with a 9.6% activity yield by DEAE-Sephacel and glutathione (GSH)-Sepharose column chromatography. The molecular weight of the enzyme was determined to be approximately 23,000 by SDS-polyacrylamide gel electrophoresis and 48,000 by gel chromatography, indicating a homodimeric...

Journal: :Journal of clinical chemistry and clinical biochemistry. Zeitschrift fur klinische Chemie und klinische Biochemie 1985
R Geiger G Leysath H Fritz

alpha 1-Proteinase inhibitor was purified from porcine blood by ammonium sulphate and Cibachron Blue-Sepharose fractionation, ion exchange chromatography on DEAE-Cellulose, gel filtration on Sephadex G-25, and zinc chelating chromatography. Thus, an inhibitor preparation with a specific activity of 1.62 IU/mg protein (enzyme: trypsin; substrate: BzArgNan) was obtained. In sodium dodecyl sulphat...

Journal: :Plant physiology 1989
V Sarafian R J Poole

An H(+)-translocating inorganic pyrophosphatase (PPase) was isolated and purified from red beet (Beta vulgaris L.) tonoplast. One major polypeptide of molecular weight 67 kilodalton copurified with fluoride-inhibitable PPase activity when subjected to one-dimensional polyacrylamide gel electrophoresis. Overall, a 150-fold purification of the PPase was obtained, from the tonoplast fraction, thro...

2003
Cell Walls

A preparative method for the isolation of oligosaccharide peptides from lysozyme digests of Micrococcus Zysodeiklicus cell walls is described. The method involves chromatography on Dowex 1, gel filtration on Bio-Gel P-4 columns, and chromatography on Dowex 50. Four glycopeptides designated as GP-1, GP-la, GP-2, and GP-4 were isolated and their structures investigated by chemical and enzymatic t...

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