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Citation Information: J Clin Invest. 1977;60(4):944-950. https://doi.org/10.1172/JCI108849.
Abstract
An arginine-rich apoprotein obtained from human triglyceride-rich lipoprotein was isolated on a heparin affinity column when either the aqueousor urea-soluble apoproteins were applied to the column. Of all the aqueous- or urea-soluble apoproteins, only this arginine-rich protein exhibited a binding affinity to heparin. This protein was eluted from the column at sodium chloride concentrations above 0.35 M in the absence of urea and between 0.17-0.2 M when isolated in urea. The protein has been characterized by amino acid analysis, immunoelectrophoresis, dodecyl sulfate polyacrylamide electrophoresis, isoelectric focusing, and NH2-terminal analysis. It has the same amino acid composition, NH2-terminal, and molecular weight as previously described for human arginine-rich apoprotein.
Authors
Frank A. Shelburne, Steven H. Quarfordt
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