𝔖 Bobbio Scriptorium
✦   LIBER   ✦

The isolation of dihydrofolate reductases by affinity chromatography on folate-Sepharose

✍ Scribed by John M. Whiteley; Gary B. Henderson; Andrea Russell; Promila Singh; Edward M. Zevely

Publisher
Elsevier Science
Year
1977
Tongue
English
Weight
653 KB
Volume
79
Category
Article
ISSN
0003-2697

No coin nor oath required. For personal study only.

✦ Synopsis

FoIate-Seph~ose at&ity column material has been prepared and used for the isolation of dihydrofolate reductases from three sources: (a) ~ethopte~n-resist~t Ll210 cells in culture; (b) amethopterin-resistant LactobaciHus casei; and (c) r To whom requests for reprints should be addressed.

πŸ“œ SIMILAR VOLUMES

Purification of guanosine triphosphate c
Purification of guanosine triphosphate cyclohydrolase I and dihydrofolate reductase on a dihydrofolate-sepharose affinity column
✍ Rudolf L. Then πŸ“‚ Article πŸ“… 1979 πŸ› Elsevier Science 🌐 English βš– 575 KB

Folate was coupled t,o AH-Sepharose 4B, the gel poured into small columns, and the Sepharose-bound folate reduced in situ to dihydrofolate by dithionite/ascorbate at pH 6 to 7. The dihydrofolate-Sepharose column was used to purify guanosine triphosphate cyclohydrolase I (EC 3.5.4.16) and dihydrofola

The purification of horseradish peroxida
The purification of horseradish peroxidase by affinity chromatography on Sepharose-bound concanavalin A
✍ Michael G. Brattain; Michael E. Marks; Thomas G. Pretlow II πŸ“‚ Article πŸ“… 1976 πŸ› Elsevier Science 🌐 English βš– 426 KB

This report describes the use of affinity chromatography on Sepharose-bound concanavalin A for the purification of horseradish peroxidase. Samples of horseradish peroxidase with A .,03:A280 ratios ranging from 0.62 to 2.45 were purified to AIOa:AZSO ratios ranging from approximately 2.8 to 3.1 with