Polyacrylamide gel electrophoresis of mycoplasma proteins in sodium dodecyl sulphate.

FOLDING OF THE INTERACTION OF HISTONE HI WITH SODIUM N-DODECYL SULPHATE

The effects of sodium n-dodecyl sulphate (SDS) on the structure of histone HI has been studied by a combination of e:quilibrium dialysis, U.V. spectroscopy ; polyacrylamide gel electrophoresis, protein titration and viscometery techniques using, 2.5 mM phosphate buffer, pH 6.4. The interaction of H, and SDS in contrast tomanyothel-protein-SDS interactions is organized between V 40 to 70. A...

IPTG isopropyl β-D-1-thiogalactopyranoside KDS potassium dodecyl sulphate LHCP light-harvesting chlorophyll-protein LP low potential LS low spin MBP maltose-binding protein MES 2-(N-Morpholino)ethanesulfonic acid OD optical density PAGE polyacrylamide gel electrophoresis PMSF phenylmethanesulfonylfluoride PS photosystem SDS sodium dodecyl sulphate

A novel mechanism of “metal gel-shift” by histidine-rich Ni-binding Hpn

23 Sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) is a universally 24 used method for determining approximate molecular weight (MW) in protein research. 25 Migration of protein that does not correlate with formula MW, termed " gel shifting " appears 26 to be common for histidine-rich proteins but not yet studied in detail. We investigated " gel 27

Molecular-weight estimates of milk-fat-globule-membrane protein-sodium dodecyl sulphate complexes by electrophoresis in gradient acrylamide gels.

The molecular weights of milk-fat-globule-membrane proteins solubilized in sodium dodecyl sulphate were estimated by gradient gel electrophoresis. Standard curves were calibrated from both protein and glycoprotein markers of known molecular weight. Six major proteins were observed with Coomassie Blue staining and six with periodic acid-Schiff staining. The behaviour of the membrane proteins and...

Affinity purification and some molecular properties of human liver alkaline phosphatase.

Alkaline phosphatase from human liver was purified to homogeneity. The purification procedure included solubilization with butanol, fractionation with acetone, and chromatography on concanavalin A-Sepharose, DEAE-cellulose, Sephadex G-200 and DEAE-Sephadex. Purity was established by standard and sodium dodecyl sulphate/polyacrylamide-gel electrophoresis. The isoelectric point of the protein was...