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Studies on Human Serum ß1-Lipoprotein

III. ENZYMATIC MODIFICATIONS

Simeon Margolis 1 and Robert G. Langdon 1

From the 1 From the Department of Physiological Chemistry, The Johns Hopkins University, School of Medicine, Baltimore, Maryland 21205

1. Exhaustive digestion of native human serum ß1-lipoprotein by either trypsin or pronase resulted in the hydrolysis of only a fraction of the potentially susceptible peptide bonds. However, hydrolysis of the lipid-free protein by these enzymes was more nearly complete.

2. Peptide maps of the products of tryptic digestion indicated that a specific segment of the polypeptide chain of the native molecule was attacked. This was supported by the observation that the amino acid composition of the soluble products resulting from either tryptic or pronase digestion differed significantly both from the parent molecule and from the residual large polypeptide component.

3. The histidine residues present in the segments attacked by trypsin or pronase were also those which were most readily modified by chemical reagents.

Submitted on July 28, 1965


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R. Prassl, J. M. Chapman, F. Nigon, M. Sara, S. Eschenburg, C. Betzel, A. Saxena, and P. Laggner
Crystallization and Preliminary X-ray Analysis of a Low Density Lipoprotein from Human Plasma
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