The solid phase synthesis of a protein activator for lecithin-cholesterol acyltransferase corresponding to human plasma apoC-I. Academic Article uri icon

Overview

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 compositions was accomplished by solid phase techniques employing a modified polystrene 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.

publication date

  • May 1, 1976

Research

keywords

  • Acyltransferases
  • Apoproteins
  • Lipoproteins, VLDL
  • Phosphatidylcholine-Sterol O-Acyltransferase
  • Phosphatidylcholines

Identity

PubMed Central ID

  • PMC430308

Scopus Document Identifier

  • 0017135639

Digital Object Identifier (DOI)

  • 10.1073/pnas.73.5.1422

PubMed ID

  • 179085

Additional Document Info

volume

  • 73

issue

  • 5