𝔖 Bobbio Scriptorium
✦   LIBER   ✦

Purification of muscle uridine diphosphoglucose pyrophosphorylase by hydrophobic chromatography

✍ Scribed by Carlo Bergamini; Marco Signorini; Carlo Ferrari; Franco Dallocchio

Publisher
Elsevier Science
Year
1984
Tongue
English
Weight
349 KB
Volume
143
Category
Article
ISSN
0003-2697

No coin nor oath required. For personal study only.

✦ Synopsis

Uridine diphosphoglucose pyrophosphorylase was purified 2500-fold from rabbit skeletal muscle with a total recovery of 35% of the initial activity. The present procedure was made possible by an extensive use of hydrophobic chromatography. Purified pyrophosphorylase had a specific activity of 500 mumol/min/mg of protein and was homogeneous by chromatographic and electrophoretic criteria. The enzyme appears to be composed of eight subunits of 53,000 molecular weight each.

πŸ“œ SIMILAR VOLUMES

Purification of some soybean proteins by
Purification of some soybean proteins by hydrophobic chromatography
✍ Senyuk, V. I. ;Yattara, H. B. ;Vaintraub, I. A. πŸ“‚ Article πŸ“… 1994 πŸ› John Wiley and Sons 🌐 English βš– 224 KB

Soybean glycinin and KUNITZ trypsin inhibitor were purified by hydrophobic chromatography on Phenyl Sepharose which removes the admixtures of more hydrophobic proteins and of some non-protein UV-absorbing substances. ## Zusammenfassung Reinigung einiger Sojabohnenproteine durch hydrophobe Chromat

Purification of human plasma retinol-bin
Purification of human plasma retinol-binding protein by hydrophobic interaction chromatography
✍ Rodolfo Berni; Simone Ottonello; Hugo L. Monaco πŸ“‚ Article πŸ“… 1985 πŸ› Elsevier Science 🌐 English βš– 332 KB

Human plasma retinol-binding protein has been purified to homogeneity by a simple method that requires an ammonium sulfate fractionation, a hydrophobic interaction chromatography on phenyl-Sepharose, which dissociates the complex between retinol-binding protein and its carrier, transthyretin, and a

Isolation of Hydrophobic Membrane Protei
Isolation of Hydrophobic Membrane Proteins by Perfusion Chromatographyβ€”Purification of Photosystem II Reaction Centers from Spinach Chloroplasts
✍ Margrit Roobol-BΓ³za; Bertil Andersson πŸ“‚ Article πŸ“… 1996 πŸ› Elsevier Science 🌐 English βš– 129 KB

Ion exchange perfusion chromatography has been teins requires the presence of detergent to solubilize introduced for the isolation of hydrophobic membrane the proteins from the lipid bilayer and to keep them protein complexes from thylakoid membranes of spinin solution during subsequent isolation. H