Detection of immunological heterogeneity of an isolated, purified protein (vervet apolipoprotein A-I).
Using a single goat antiserum, we have identified immunological heterogeneity of purified apolipoprotein A-I from high density lipoprotein of vervet monkeys. We examined whether the apparent heterogeneity was due to separate antigenic sites within the polypeptide sequence or rather on the different isoproteins, which result in charge heterogeneity of this protein. The apolipoprotein A-I was cleaved with cyanogen bromide and the resulting three fragments were purified and characterized. By using immunodiffusion, each of the fragments was found to show a characteristic and different reaction to the antiserum. By contrast, apparent identity was found by immunodiffusion among the separate isoprotein forms of apolipoprotein A-I. We have concluded that the immunological heterogeneity of apolipoprotein A-I was due to different antigenic sites within the primary sequence of apolipoprotein A-I.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D016632:Apolipoprotein A-I; D001053:Apolipoproteins / Q000276:immunology* / Q000302:isolation & purification; D002522:Chlorocebus aethiops; D003429:Cross Reactions; D000939:Epitopes; D000882:Haplorhini; D005779:Immunodiffusion; D007525:Isoelectric Focusing
D000596:Amino Acids; D016632:Apolipoprotein A-I; D001053:Apolipoproteins; D000939:Epitopes