Use of dimethyl suberimidate, a cross-linking reagent, in studying the subunit structure of oligomeric proteins - PubMed (original) (raw)

Use of dimethyl suberimidate, a cross-linking reagent, in studying the subunit structure of oligomeric proteins

G E Davies et al. Proc Natl Acad Sci U S A. 1970 Jul.

Abstract

Amidination of aldolase, glyceraldehyde-3-phosphate dehydrogenase, tryptophan synthetase B protein, L-arabinose isomerase, and the catalytic subunit of E. coli aspartate transcarbamylase with the bifunctional reagent dimethyl suberimidate produces cross-linked proteins, with reaction predominating within oligomers. Disc electrophoresis of a modified protein on polyacrylamide gel in the presence of sodium dodecyl sulfate resolves a set of species with molecular weights equal to integral multiples of the protomer molecular weight. For oligomers composed of identical protomers, the number of principal species observed is identical to the number of protomers in the oligomer. Application of the method to two proteins composed of dissimilar protomers, native aspartate transcarbamylase and tryptophan synthetase alpha(2)beta(2) complex of E. coli, revealed differences in the reactivities of the different kinds of protomer within each oligomer.

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References

    1. J Biol Chem. 1966 Feb 25;241(4):980-90 - PubMed
    1. Biochem Biophys Res Commun. 1966 Jun 13;23(5):730-9 - PubMed
    1. J Biol Chem. 1967 Jun 25;242(12):2886-92 - PubMed
    1. Biochemistry. 1967 Aug;6(8):2439-48 - PubMed
    1. Biochem Biophys Res Commun. 1967 Sep 7;28(5):815-20 - PubMed

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