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Bovine Liver Thiol-Protein Disulphide Oxidoreductases. An Alternative Method for Differential Purification and Resolution of Protein Disulphide-Isomerase and Glutathione-Insulin Transhydrogenase

Bovine Liver Thiol-Protein Disulphide Oxidoreductases. An Alternative Method for Differential Purification and Resolution of Protein Disulphide-Isomerase and Glutathione-Insulin Transhydrogenase

D A Hillson, R B Freedman

Biochem J. 1980 Nov 1;191(2):389-93.

PMID: 7236203

Abstract:

1. Protein disulphide-isomerase (EC 5.3.4.1) and glutathione-insulin transhydrogenase (EC 1.8.4.2) activities in bovine liver were studied in parallel during purification of 'thiol-protein disulphide oxidoreductase' by the procedure of Carmichael, Morin & Dixon [(1977) J Biol. Chem. 252, 7163-7167]. The two activities showed no quantitative co-purification and were partially resolved by (NH4)SO4 precipitation, indicating that distinct enzymes are present. 2. Protein disulphide-isomerase was purified by a relatively rapid method involving a combination of the early stages of the Carmichael procedure and covalent chromatography, with a new stepwise elution procedure. Ion-exchange chromatography yields a homogeneous preparation of mol.wt. 57 000. 3. The relationship between protein disulphide-isomerase, glutathione-insulin transhydrogenase and 'thiol-protein disulphide oxidoreductase' is discussed.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP37318493	Protein Disulfide Isomerase from bovine liver		37318-49-3	Price

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