Separation of HMG proteins by reverse-phase HPLC
A high-pressure liquid chromatographic method is described for separating the high mobility group (HMG) proteins on a 5-..mu..m Nucleosil C18 column with the use of the ion pairing agent trifluoroacetic acid (TFA) in the mobile phase. With a multistep acetonitrile-TFA gradient, the calf thymus HMG proteins elute from this column as separate peaks in the order HMG 17, 14, 2, and 1. Protein elution is monitored by measuring the absorbance at 214 nm in a 3-mm flow cell, and the identity and purity of the peaks are confirmed by polyacrylamide gel electrophoresis and amino acid analysis. Both HMG 1 and 2 elute as multiple peaks, suggesting the presence of major variants of these two proteins. Other peaks in the chromatogram include degradation products of HMG 1 and histone H1. 12 references, 1 figure, 1 table.
- Research Organization:
- Lawrence Livermore National Lab., CA
- DOE Contract Number:
- W-7405-ENG-48
- OSTI ID:
- 5944168
- Journal Information:
- J. Liquid Chromatogr.; (United States), Journal Name: J. Liquid Chromatogr.; (United States) Vol. 7:5; ISSN JLCHD
- Country of Publication:
- United States
- Language:
- English
Similar Records
High mobility group protein number17 cross-links primarily to histone H2A in the reconstituted HMG 17 - nucleosome core particle complex
Histone fractionation by high-performance liquid chromatography on cyanoalkylsilane (CN) reverse-phase columns
Related Subjects
59 BASIC BIOLOGICAL SCIENCES
AMINO ACIDS
ANIMALS
BODY
CALVES
CARBOXYLIC ACIDS
CATTLE
CHROMATOGRAPHY
DATA
DOMESTIC ANIMALS
ELECTROPHORESIS
EXPERIMENTAL DATA
INFORMATION
LIQUID COLUMN CHROMATOGRAPHY
LYMPHATIC SYSTEM
MAMMALS
NUMERICAL DATA
ORGANIC ACIDS
ORGANIC COMPOUNDS
ORGANS
PROTEINS
RUMINANTS
SEPARATION PROCESSES
THYMUS
VERTEBRATES