Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
175004 | Data in Brief | 2016 | 6 Pages |
Abstract
GroEL chaperonin is well-known to interact with a wide variety of polypeptide chains. Here we show the data related to our previous work (http://dx.doi.org/10.1016/j.pep.2015.11.020[1]), and concerning the interaction of GroEL with native (lysozyme, α-lactalbumin) and denatured (lysozyme, α-lactalbumin and pepsin) proteins in solution. The use of affinity chromatography on the base of denatured pepsin for GroEL purification from fluorescent impurities is represented as well.
Related Topics
Physical Sciences and Engineering
Chemical Engineering
Chemical Engineering (General)
Authors
V.V. Marchenkov, N.Yu. Marchenko, A.L. Kaysheva, N.V. Kotova, I.A. Kashparov, G.V. Semisotnov,