| Literature DB >> 2613776 |
T Oeda1, A Hirai, T Ban, Y Tamura, S Yoshida.
Abstract
The application of TSK-Toyopearl gels to the preparative separation of a basic and low-molecular-weight protein, sterol carrier protein2 (SCP2), was studied. SCP2 was purified from 105,000 g supernatant of rat liver (S105) by ion-exchange chromatography on CM-Toyopearl 650M and gel permeation on Toyopearl HW60S. Separation of S105 by CM-Toyopearl 650M was carried out at a high flow-rate in the presence of 10% (v/v) glycerol, a stabilizer of the protein. Toyopearl HW60S showed a significant ion-exchange effect on the elution of SCP2. Using an elution buffer of ionic strength of 45 mM, a highly efficient purification of SCP2 on HW60S was achieved. SCP2 was purified approximately 5000-fold to apparent homogeneity with an overall yield of 69%.Entities:
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Year: 1989 PMID: 2613776 DOI: 10.1016/s0021-9673(01)93212-1
Source DB: PubMed Journal: J Chromatogr