Post-translational heterogeneity of the human vitamin D-binding protein (group-specific component)

Dorian H. Coppenhaver, Nicholas P. Sollenne, Barbara H. Bowman

Research output: Contribution to journalArticle

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Abstract

The vitamin D-binding protein in human serum (the group-specific component) is an α2-globulin which is genetically polymorphic in all populations studied. Previous work (J. Svasti and B. H. Bowman (1978) J. Biol. Chem. 253, 5188-5194, and J. Svasti, A. Kurosky, A. Bennett, and B. H. Bowman (1979) Biochemistry 18, 1611-1617) has shown that the electrophoretic variations of the proteins controlled by two allelic genes, Gc1 and Gc2, are due to at least three amino acid substitutions between Gc1 and Gc2 (Svasti et al. (1979)) and to heterogeneity in the Gc1 phenotype arising from carbohydrate dissimilarities. Gc1 migrates electrophoretically as two protein bands, while Gc2 migrates cathodally as a single band. This study demonstrates a post-translational glycosylation difference occurring in a single area of the Gc1 sequence which accounts for the heterogeneity observed previously. The glycosylation site, a threonine residue, appears to be in a sequence which differs between Gc1 and Gc2. The O-glycosidic bond, which is typical of mucins, is rare in plasma proteins. The cyanogen bromide fragment containing the galactosamine-containing carbohydrate in Gc1 was partially sequenced through 20 residues from the amino terminus. No detectable galactosamine could be found in the homologous cyanogen bromide fragment in Gc2. A new purification procedure for the vitamin D-binding protein in human plasma has been developed. Three chromatographic steps provide purified protein.

Original languageEnglish (US)
Pages (from-to)218-223
Number of pages6
JournalArchives of Biochemistry and Biophysics
Volume226
Issue number1
DOIs
StatePublished - Oct 1 1983

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Vitamin D-Binding Protein
Glycosylation
Cyanogen Bromide
Galactosamine
Carbohydrates
Plasma (human)
Biochemistry
Proteins
Globulins
Mucins
Threonine
Amino Acid Substitution
Purification
Blood Proteins
Substitution reactions
Genes
Phenotype
Amino Acids
Serum
Population

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Post-translational heterogeneity of the human vitamin D-binding protein (group-specific component). / Coppenhaver, Dorian H.; Sollenne, Nicholas P.; Bowman, Barbara H.

In: Archives of Biochemistry and Biophysics, Vol. 226, No. 1, 01.10.1983, p. 218-223.

Research output: Contribution to journalArticle

Coppenhaver, Dorian H. ; Sollenne, Nicholas P. ; Bowman, Barbara H. / Post-translational heterogeneity of the human vitamin D-binding protein (group-specific component). In: Archives of Biochemistry and Biophysics. 1983 ; Vol. 226, No. 1. pp. 218-223.
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