Cyst(e)ine residues of bovine white-matter proteolipid proteins. Role of disulphides in proteolipid conformation.

P. I. Oteiza, A. M. Adamo, P. A. Aloise, A. C. Paladini, A. A. Paladini, E. F. Soto

Research output: Contribution to journalArticle

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Abstract

Cyst(e)ine residues of bovine white-matter proteolipid proteins were characterized in a highly purified preparation. From a total of 10.6 cyst(e)ine residues/molecule of protein, as determined by performic acid oxidation, 2.5-3 thiol groups were freely accessible to iodoacetamide, iodoacetic acid and 5,5'-dithiobis-(2-nitrobenzoic acid) (DTNB), when the proteins were solubilized in chloroform/methanol (C/M) (2:1, v/v). The presence of lipids had no effect on thiol-group exposure. One thiol group available to DTNB in C/M could not be detected when proteolipids were solubilized in the more polar solvent n-butanol. In a C/M solution of purified proteolipid proteins, SDS did not increase the number of reactive thiol groups, but the cleavage of one disulphide bridge made it possible to alkylate six more groups. C.d. and fluorescence studies showed that rupture of this disulphide bond changed the protein conformation, which was reflected in partial loss of helical structure and in a greater exposure to the solvent of at least one tryptophan residue. Cyst(e)ine residues were also characterized in the different components [PLP (principal proteolipid protein), DM20 and LMW (low-Mr proteins)] of the proteolipid preparation. Although the numbers of cyst(e)ine residues in PLP and DM20 were similar, in LMW fewer residues were alkylated under four different experimental conditions. The differences, however, are not simply related to differences in Mr.

Original languageEnglish (US)
Pages (from-to)507-513
Number of pages7
JournalBiochemical Journal
Volume245
Issue number2
StatePublished - Jul 15 1987
Externally publishedYes

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Proteolipids
Disulfides
Conformations
Cysts
Dithionitrobenzoic Acid
Sulfhydryl Compounds
Chloroform
Methanol
Proteins
Iodoacetic Acid
Iodoacetamide
Protein Conformation
1-Butanol
Tryptophan
White Matter
Rupture
Fluorescence
Lipids
Oxidation
Molecules

ASJC Scopus subject areas

  • Biochemistry

Cite this

Oteiza, P. I., Adamo, A. M., Aloise, P. A., Paladini, A. C., Paladini, A. A., & Soto, E. F. (1987). Cyst(e)ine residues of bovine white-matter proteolipid proteins. Role of disulphides in proteolipid conformation. Biochemical Journal, 245(2), 507-513.

Cyst(e)ine residues of bovine white-matter proteolipid proteins. Role of disulphides in proteolipid conformation. / Oteiza, P. I.; Adamo, A. M.; Aloise, P. A.; Paladini, A. C.; Paladini, A. A.; Soto, E. F.

In: Biochemical Journal, Vol. 245, No. 2, 15.07.1987, p. 507-513.

Research output: Contribution to journalArticle

Oteiza, PI, Adamo, AM, Aloise, PA, Paladini, AC, Paladini, AA & Soto, EF 1987, 'Cyst(e)ine residues of bovine white-matter proteolipid proteins. Role of disulphides in proteolipid conformation.', Biochemical Journal, vol. 245, no. 2, pp. 507-513.
Oteiza PI, Adamo AM, Aloise PA, Paladini AC, Paladini AA, Soto EF. Cyst(e)ine residues of bovine white-matter proteolipid proteins. Role of disulphides in proteolipid conformation. Biochemical Journal. 1987 Jul 15;245(2):507-513.
Oteiza, P. I. ; Adamo, A. M. ; Aloise, P. A. ; Paladini, A. C. ; Paladini, A. A. ; Soto, E. F. / Cyst(e)ine residues of bovine white-matter proteolipid proteins. Role of disulphides in proteolipid conformation. In: Biochemical Journal. 1987 ; Vol. 245, No. 2. pp. 507-513.
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