SUBUNIT HETEROGENEITY IN HUMAN SERUM BETA LIPOPROTEIN

Abstract
The apoprotein of human serum beta lipoprotein has been prepared in a lipid-free and soluble form by a technique of interfacial extraction in the presence of guanidinium hydrochloride and nonionic amphiphile. Gel permeation chromatography of maleylated apobeta lipoprotein separates two protein fractions with different amino acid compositions. The smaller particle has a molecular weight of 2.6 x 10(4).