Physical heterogeneity of bovine γ-globulins

Characterization of γM and γG globulins

Frederick A. Murphy, John W. Osebold, Ole Aalund

Research output: Contribution to journalArticle

23 Citations (Scopus)

Abstract

The γG globulins of bovine serum were characterized by anion exchange chromatography, immunoelectrophoresis, zone electrophoresis, ultracentrifugation, and analysis of the products of papain digestion. Their properties were similar to those of analogous components of human serum. Fast and slow γG globulins were distinguished on the basis of differences in electrophoretic migration rates, chromatographic elution positions, and biological activities (complement fixation). Antigenic differences were detectable only in immunoelectrophoretic patterns (spur formation). Bovine γM was found to have properties quite similar to those of the analogous protein in human serum as determined by the methods of gel filtration, immunoelectrophoresis, anion exchange chromatography, ultracentrifugation, and reduction with mercaptoethanol. Bovine γA was provisionally recognized in immunoelectrophoretic analyses of serum and chromatographic fractions.

Original languageEnglish (US)
Pages (from-to)126-136
Number of pages11
JournalArchives of Biochemistry and Biophysics
Volume112
Issue number1
StatePublished - Oct 1965

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Globulins
Chromatography
Anions
Immunoelectrophoresis
Ultracentrifugation
Papain
Mercaptoethanol
Bioactivity
Electrophoresis
Serum
Serum Globulins
Ion exchange
Gels
Gel Chromatography
Digestion
Proteins

ASJC Scopus subject areas

  • Molecular Biology
  • Biophysics
  • Biochemistry

Cite this

Physical heterogeneity of bovine γ-globulins : Characterization of γM and γG globulins. / Murphy, Frederick A.; Osebold, John W.; Aalund, Ole.

In: Archives of Biochemistry and Biophysics, Vol. 112, No. 1, 10.1965, p. 126-136.

Research output: Contribution to journalArticle

Murphy, Frederick A. ; Osebold, John W. ; Aalund, Ole. / Physical heterogeneity of bovine γ-globulins : Characterization of γM and γG globulins. In: Archives of Biochemistry and Biophysics. 1965 ; Vol. 112, No. 1. pp. 126-136.
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