Activated CH-Sepharose 4B and protein A Sepharose CL-4B can bind, selectively and non-specifically, polypeptides from chick embryo cells. The major polypeptides bound have apparent molecular masses of 57-60 kDa and 47-49 kDa and cannot be eluted by extensive washing with buffers containing detergent
Fractionation of nonhistone proteins on a column of daunomycin-CH-sepharose 4B
β Scribed by Hideaki Kikuchi; Shojiro Sato
- Book ID
- 113125794
- Publisher
- Elsevier Science
- Year
- 1978
- Weight
- 481 KB
- Volume
- 532
- Category
- Article
- ISSN
- 0005-2795
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A procedure is described for the determination of the Stokes radius of a detergent micelie by gel chromatography. It was observed that different lots of Sepharose -4B can exhibit a wide variation in the permeation of their gel pores. It is shown that this variation is due to differences in their por
Affinity Chromatography of Aspergillus Acid Proteinase on an ~,O-Dibenzy~oxycarbonyi-~yrosine-AH-Sepharose 4B Column N,O-dibenzyloxycarbonyl-L-tyrosine Z-Tyr(Z) has been found to be a specific inhibitor of Aspergiiius acid proteinase and was coupled with hexamethylene-diamin~sepharose 4B (AH-Sepharo