Isolation, purification & properties of lactose binding agglutination factor from rabbit skeletal muscle.
The lactose binding agglutination factor from rabbit skeletal muscle is isolated through the use of lactose and urea. The factor is purified with DEAE cellulose and Sepharose 4B chromatography. The molecular weight of the factor is determined with Sephadex G-75 chromatography and found to be 28,000 Daltons. The subunit's molecular weight is determined by SDS gel electrophoresis, and found to be 14,000 Daltons. It was found that this binding factor can agglutinate trypsin-treated rabbit erythrocytes. Moreover, this agglutination is inhibited by EDTA and lactose.
D000818:Animals; D007611:Aprotinin / Q000494:pharmacology; D002848:Chromatography, DEAE-Cellulose; D002850:Chromatography, Gel; D004492:Edetic Acid / Q000494:pharmacology; D004591:Electrophoresis, Polyacrylamide Gel; D037541:Galectin 4; D006384:Hemagglutination / Q000187:drug effects; D006388:Hemagglutinins / Q000302:isolation & purification*; D007785:Lactose / Q000378:metabolism*; D008970:Molecular Weight; D009132:Muscles / Q000032:analysis*; D011817:Rabbits
D037541:Galectin 4; D006388:Hemagglutinins; D007611:Aprotinin; D004492:Edetic Acid; D007785:Lactose