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Study on the interactions between protein disulfide isomerase and target proteins, using immobilization on solid support
Author(s) -
Muronetz Vladimir I,
Zhang Nian Xian,
Bulatnikov Igor G,
Wang Chih-Chen
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)00319-6
Subject(s) - protein disulfide isomerase , chemistry , glyceraldehyde 3 phosphate dehydrogenase , monomer , biochemistry , enzyme , lysozyme , isomerase , sepharose , chaperone (clinical) , dehydrogenase , organic chemistry , polymer , medicine , pathology
Interaction between protein disulfide isomerase, possessing not only isomerase but also chaperone‐like activity, and olygomeric enzyme, GAPDH, has been studied using technique of immobilization on insoluble support. PDI dimers bound to CNBr‐activated Sepharose were shown to posses high TPOR activity as well as the ability to reactivate lysozyme. Immobilized PDI was not found to interact neither with soluble tetrameric GAPDH, nor with soluble denatured GAPDH. However, soluble PDI binds effectively to immobilized GAPDH monomers; K d was found to be 3.7×10 −6 M, stoichiometry 0.824 mole PDI monomers per mole GAPDH monomers. Immobilized GAPDH tetramers do not interact with PDI. These observations are also confirmed by the data on electrophoresis of proteins bound to immobilized GAPDH monomers and tetramers. The ability of PDI to interact with denatured protein form, but not with the native one, is considered to be evidence of chaperone‐like activity of the enzyme.