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J. Biochem, 1977, Vol. 81, No. 4 955-961
© 1977 Japanese Biochemical Society

research-article

Proteolysis of Apoproteins in Human Serum Low Density Lipoprotein1

Atsushi IKAI and Hitoshi YAGISAWA

Department of Biochemistry, Faculty of Science, University of Tokyo Hongo, Bunkyo-ku, Tokyo 113

Proteolytic treatment of human serum low density lipoprotein (LDL) resulted in the observati-on of interesting time-dependent changes in the sodium dodecyl sulfate-polyacrylamide gel electrophoretic pattern of apo-LDL. Five major fragments with well-defined relative mobilities appeared within 30 min of protease treatment. Prolonged treatment with subtilisin caused changes in the amount of peptides in each of the five bands but their positions on the gel remained unchanged. Periodic acid-Schiff base staining of the gel showed a proteolytic fragment with an apparent molecular weight of 110,000 (actually a cross-linked dimer of two peptides with molecular weights of 77,000 and 68,000) to be a carbohydrate-bearing peptide that was most resistant to further proteolysis and therefore responsible for the interaction between the digested LDL and concanavalin A.

1This work was supported in part by a research grant from the Kurata Science Foundation to Atsushi Ikai.


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