نتایج جستجو برای: sds polyacrylamide gel electrophoresis

تعداد نتایج: 131538  

Journal: :Journal of animal science 1996
E Huff-Lonergan T Mitsuhashi F C Parrish R M Robson

Purified myofibril (MF) and homogenized whole muscle (WM) samples were prepared from A maturity market steers. Samples were removed at 0, 1, 3, 7, 14, and 28 d postmortem. The MF and WM samples from all steers were analyzed by SDS-PAGE (5% gels) and by Western blot analysis using monoclonal antibodies to titin and nebulin. The rates of degradation of the intact forms of titin and nebulin, with ...

Journal: :Journal of bacteriology 1992
T J Han T J Chai

Lipopolysaccharides (LPSs) isolated from three Kanagawa-positive and three negative strains of Vibrio parahaemolyticus were characterized by using electrophoretic, immunochemical, and chemical methods. The results of this study indicated that the LPSs of all six strains of V. parahaemolyticus examined did not have an O-specific side chain. These V. parahaemolyticus LPSs appeared to have molecul...

Journal: :The Journal of biological chemistry 1992
S E Bennett D W Mosbaugh

The Bacillus subtilis bacteriophage PBS2 uracil-DNA glycosylase inhibitor (Ugi) protein was characterized and shown to form a stable complex with Escherichia coli uracil-DNA glycosylase (Ung). As determined by mass spectrometry, the Ugi protein had a molecular weight of 9,474. We confirmed this value by sedimentation equilibrium centrifugation and determined that Ugi exists as a monomeric prote...

Journal: :The Journal of antibiotics 1988
T Otani Y Minami T Marunaka R Zhang M Y Xie

A new macromolecular antibiotic C-1027 was obtained from the broth filtrate of Streptomyces globisporus C-1027 by precipitation with ammonium sulfate, DEAE-cellulose column chromatography and gel filtration chromatography on a Sephadex G-75 column. This antibiotic, prepared as a white powder, is an acidic polypeptide having an isoelectric point of pH 3.5-3.7 and a molecular weight of 15,000 as ...

Journal: :Journal of reproduction and fertility 1983
C R Brown

When proacrosin from mouse epididymal spermatozoa was activated a single form of acrosin was produced. The enzyme was isolated by gel filtration followed by affinity chromatography using Sepharose-4B linked to an acrosin inhibitor p-(p'-aminophenoxypropoxy)benzamidine. The molecular weight of partly purified acrosin was 53 000 by gel filtration, and of the pure enzyme 39 000 by SDS-polyacrylami...

Journal: :Clinical chemistry 1980
P M Clark L J Kricka T P Whitehead

Characteristic differences in the pattern of urinary proteins and peptides have been found in patients with rheumatoid arthritis, compared with patterns from healthy controls. These differences have been demonstrated with a two-dimensional gel electrophoretic technique (Iso-Dalt) involving isoelectric focusing in the first dimension, followed by sodium dodecyl sulfate-polyacrylamide gel electro...

Journal: :Plant physiology 1979
R E Hunt L H Pratt

We have developed a phytochrome immunoaffinity purification procedure that yields undegraded oat (Avena sativa L., cv. Garry) phytochrome of greater than 98% purity within 2 hours when starting with a brushite-purified preparation. Immunoaffinity-purified phytochrome, except for its greater purity, is indistinguishable from conventionally purified phytochrome by gel exclusion chromatography, is...

Journal: :Analytical biochemistry 1987
H Schägger G von Jagow

A discontinuous sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) system for the separation of proteins in the range from 1 to 100 kDa is described. Tricine, used as the trailing ion, allows a resolution of small proteins at lower acrylamide concentrations than in glycine-SDS-PAGE systems. A superior resolution of proteins, especially in the range between 5 and 20 kDa, is ach...

Journal: :Folia parasitologica 2000
M Slovák V Hajnická M Labuda N Fuchsberger

Salivary gland extracts (SGE) from unfed and 5 days fed adult female Ixodes ricinus (Linnaeus, 1758); Haemaphysalis inermis (Birula, 1895) and Dermacentor reticulatus (Fabricius, 1794) ticks were prepared. The protein content after feeding increased by 10.6, 8.7 and 6.8 times, respectively. Extracts were equilibrated to the same protein content and submitted to SDS-polyacrylamide gel electropho...

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