𝔖 Bobbio Scriptorium
✦   LIBER   ✦

Concentration-dependent migration in gel chromatography of reversibly polymerizing solutes: the osmotic behavior of polyacrylamide gels

✍ Scribed by Ross Tellam; Donald J. Winzor

Book ID
103670444
Publisher
Elsevier Science
Year
1980
Tongue
English
Weight
751 KB
Volume
12
Category
Article
ISSN
0301-4622

No coin nor oath required. For personal study only.

📜 SIMILAR VOLUMES

The Effect of Solute Concentration on Eq
The Effect of Solute Concentration on Equilibrium Partitioning in Polymeric Gels
✍ Kristan K.S. Buck; Natalia I. Gerhardt; Stephanie R. Dungan; Ronald J. Phillips 📂 Article 📅 2001 🏛 Elsevier Science 🌐 English ⚖ 129 KB

The effect of solute concentration on the equilibrium partitioning of sphere-like, colloidal solutes in stiff polymer hydrogels is examined theoretically and experimentally. The theoretical development is a statistical mechanics approach, and allows quantitative calculations to be performed to deter

Kinetics of radical polymerization—XLVI:
Kinetics of radical polymerization—XLVI: Kinetic investigation of the polymerization of styrene in solution by gel permeation chromatography
✍ M. Szesztay; T. Földes-Berezsnich; F. Tüdös; Zs. László-Hedvig 📂 Article 📅 1985 🏛 Elsevier Science 🌐 English ⚖ 433 KB

Molecular mass distribution was investigated for the polymerization of styrene initiated by AIBN at 50 in the presence of various solvents. Two types of solvents were chosen; in one, there is no chain transfer to solvent (Bz, DMF) whereas in CC14 the chain transfer should be considered. The molecula

Reevaluation of the Electrophoretic Migr
Reevaluation of the Electrophoretic Migration Behavior of Soluble Globular Proteins in the Native and Detergent-Denatured States in Polyacrylamide Gels
✍ Willem H.J. Westerhuis; James N. Sturgis; Robert A. Niederman 📂 Article 📅 2000 🏛 Elsevier Science 🌐 English ⚖ 124 KB

Although sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis is widely used for estimating molecular masses of proteins, considerable uncertainty still exists both about the structure of SDSprotein complexes and about their mechanism of electrophoretic migration. In this study, soluble g

Chromatography of glycosaminoglycans on
Chromatography of glycosaminoglycans on hydrophobic gel. Correlation between chromatographic behavior of glycosaminoglycans on phenyl-sepharose CL-4B and their solubility in the presence of high concentrations of ammonium sulfate
✍ Hideki Uchiyama; Kimiyo Okouchi; Kinzo Nagasawa 📂 Article 📅 1985 🏛 Elsevier Science 🌐 English ⚖ 752 KB

The effect of bound sulfate groups and uronic acid residues of glycosaminoglycans on their behavior in chromatography on hydrophobic gel was examined by the use of several pairs of depolymerized chondroitin, chondroitin 4- or 6-sulfate, and dermatan sulfate having comparable degree of polymerization