Dog alpha-1-acid glycoprotein: purification and biochemical characterization.
Dog alpha-1-acid glycoprotein was purified to homogeneity from dog serum in a three-step procedure involving precipitation with sulphosalicylic acid, isoelectric focusing and size exclusion chromatography. The molecular heterogeneity in the peptide part and in the carbohydrate part of the molecule was investigated with analytical isoelectric focusing in a narrow pH range and crossed immunoaffinity electrophoresis with concanavalin A (con A) in the first-dimension gel. Up to seven molecular forms with different isoelectric points were found, whereas only a single con A-dependent molecular form was detected.
Heymans Institute of Pharmacology, Medical School, Univeristy of Ghent, Belgium.
C P
CP
Dello
F M
FM
Belpaire
J A
JA
Kint
N H
NH
Fraeyman
D000818:Animals; D003208:Concanavalin A / Q000494:pharmacology; D004285:Dogs; D007123:Immunoelectrophoresis, Two-Dimensional; D007202:Indicators and Reagents; D007525:Isoelectric Focusing; D009961:Orosomucoid / Q000032:analysis / Q000276:immunology / Q000302:isolation & purification*; D010096:Oxprenolol / Q000378:metabolism; D011485:Protein Binding
D007202:Indicators and Reagents; D009961:Orosomucoid; D003208:Concanavalin A; D010096:Oxprenolol