Composition and genetic variability of heparin-sepharose CL-6B protein fractions obtained from the solubilized proteins of mouse organs.
The solubilized proteins of liver and brain from mice of two inbred strains (C57BL/6J and DBA/2J) and their hybrids were subfractionated by heparin Sepharose (H-S) CL-6B affinity chromatography. The H-S binding and nonbinding proteins were separated by two-dimensional electrophoresis. The protein patterns obtained were analyzed with regard to their protein composition and their genetic variability (qualitative and quantitative variants). Eighty to ninety percent of the H-S binding proteins were unique to this class of proteins. This class was rich in organ-specific proteins. Compared to the nonbinding proteins the portion of basic proteins was only slightly increased, suggesting that most of the H-S binding proteins interact specifically with heparin. The frequency of qualitative protein variants revealed that H-S binding proteins are more conservative than H-S nonbinding proteins. The quantitative genetic variability was higher in liver than in brain. Quantitative protein variants occurred more frequently than qualitative variants.
D000818:Animals; D001923:Brain Chemistry; D002846:Chromatography, Affinity; D005260:Female; D006493:Heparin / Q000378:metabolism*; D007526:Isoelectric Point; D008099:Liver / Q000032:analysis*; D051379:Mice; D008810:Mice, Inbred C57BL; D008811:Mice, Inbred DBA; D008970:Molecular Weight; D011506:Proteins / Q000032:analysis* / Q000378:metabolism; D012685:Sepharose / Q000031:analogs & derivatives; D012995:Solubility
D011506:Proteins; C037405:heparin-sepharose; D006493:Heparin; D012685:Sepharose