The solid phase synthesis of a protein activator for lecithin cholesterol acyltransferase corresponding to human plasma apoC I

G. F. Sigler, A. K. Soutar, L. D. Smith, Antonio Gotto, J. T. Sparrow

Research output: Contribution to journalArticle

24 Scopus citations

Abstract

Apolipoprotein C I, a protein constituent of the very low density lipoproteins of human plasma, consists of a single chain of 57 amino acids. The total synthesis of a protein corresponding to apolipoprotein C I in physical properties and composition was accomplished by solid phase techniques employing a modified polystyrene incorporating spacer groups between the point of attachment of the first residue and the polymer matrix. The synthetic apoprotein was shown to activate lecithin:cholesterol acyltransferase to the same extent as the native protein. Comparative lipid binding studies with dimyristoyl phosphatidylcholine gave complexes for native and synthetic apoprotein which floated at the same density after ultracentrifugation in KBr gradients and had virtually the same lipid:protein ratios.

Original languageEnglish (US)
Pages (from-to)1422-1426
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume73
Issue number5
DOIs
StatePublished - 1976

ASJC Scopus subject areas

  • General

Fingerprint Dive into the research topics of 'The solid phase synthesis of a protein activator for lecithin cholesterol acyltransferase corresponding to human plasma apoC I'. Together they form a unique fingerprint.

Cite this