نتایج جستجو برای: polyacrylamide gel

تعداد نتایج: 106961  

2001
Heidrun Matern Siegfried Matern Wolfgang Gerok Christa Schelzig Helmut Holzer

Microsomal UDP-glucuronosyltransferase activity toward chenodeoxycholic acid and testosterone has been isolated from rat liver and appears to be homogeneous in sodium dodecyl sulfate gel electrophoresis and polyacrylamide gradient gel electrophoresis. The conjugating activities toward chenodeoxycholic acid and testosterone co-purified and showed identical mobilities in disc gel electrophoresis,...

Journal: :Clinical chemistry 1989
J T Wu R K Pieper L H Wu J L Peters

We isolated myoglobin from sheep heart by homogenizing cardiac muscle in 70%-saturated ammonium sulfate, followed by chromatography on a column containing carboxymethyl(CM)-Sephadex gel. Two major isoforms of myoglobin, designated Mb 7.9 and Mb 8.1, were separated by chromatofocusing and were distinguished by their different patterns seen on either isoelectrofocusing or on electrophoresis on po...

Journal: :The Biochemical journal 1981
F A Firgaira R G Cotton D M Danks

Dihydropteridine reductase (EC 1.6.99.7) was purified from human liver obtained at autopsy by a three-step chromatographic procedure with the use of (1) a naphthoquinone affinity adsorbent, (2) DEAE-Sephadex and (3) CM-Sephadex. The enzyme was typically purified 1000-fold with a yield of 25%. It gave a single band on non-denaturing and sodium dodecyl sulphate/polyacrylamide-gel electrophoresis,...

Journal: :The Journal of biological chemistry 1982
H Matern S Matern W Gerok

Microsomal UDP-glucuronosyltransferase activity toward chenodeoxycholic acid and testosterone has been isolated from rat liver and appears to be homogeneous in sodium dodecyl sulfate gel electrophoresis and polyacrylamide gradient gel electrophoresis. The conjugating activities toward chenodeoxycholic acid and testosterone co-purified and showed identical mobilities in disc gel electrophoresis,...

Journal: :BioTechniques 1996
G Zeng T J Larson

similar yield as the standard method. Therefore, using this modified method, we can reduce the soaking time from 15 h to about 10 min. In summary, a simple modification of the crush-and-soak method allows the recovery of ODN from polyacrylamide gel within 30 min with high yield. The key difference in our procedure is the replacement of the overnight soak with a heat/freeze step (summarized in T...

Earthworms possess antioxidant, antibacterial, antitumor, and hemolytic properties. To recognize the molecules responsible for various biological activities of earthworm’s coelomic fluid, a detailed knowledge about its protein contents is required. The aim of this study was to characterize the proteins present within the coelomic fluid of Eisenia foetida earthworm. Polyacrylamide-gel-elec...

Journal: :Journal of visualized experiments : JoVE 2012
Alexander C Hwang Paris H Grey Katrina Cuddy David G Oppenheimer

The evaluation of proteins using sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) analysis is a common technique used by biochemistry and molecular biology researchers. For laboratories that perform daily analyses of proteins, the cost of commercially available polyacrylamide gels (~$10/gel) can be considerable over time. To mitigate this cost, some researchers prepare their...

Journal: :Plant physiology 1993
J Grenier C Potvin A Asselin

Proteins from intercellular fluid extracts of chemically stressed barley (Hordeum vulgare L.) leaves were separated by native polyacrylamide gel electrophoresis at alkaline or acid pH. Polyacrylamide gels contained Saccharomyces cerevisiae (bakers' yeast) or Schizosaccharomyces pombe (fission yeast) crude cell walls for assaying yeast wall lysis. In parallel, gels were overlaid with a suspensio...

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