The primary structure of high density apolipoprotein glutamine I Academic Article uri icon

Overview

MeSH Major

  • Amino Acid Sequence
  • Apoproteins
  • Glutamine
  • Lipoproteins, HDL

abstract

  • The major protein constituent of human plasma high density lipoproteins has been isolated and its complete amino-acid sequence determined. The protein, designated apolipoprotein-glutamine-I by the presence of carboxyl-terminal glutamine, is a single polypeptide chain of 245 amino-acid residues, including three residues of methionine. The protein is devoid of cysteine, cystine, and isoleucine. Cleavage of apolipoprotein-glutamine-I with cyanogen bromide yields four fragments with 94, 90, 36, and 25 amino acids. The amino-acid sequence of each fragment was determined by conventional methods, with proteolytic digestion with trypsin, chymotrypsin, and thermolysin. The alignment of the cyanogen bromide fragments was determined by the isolation of the methionine-containing tryptic peptides from apolipoprotein-glutamine-I. Inspection of the sequence of apolipoprotein-glutamine-I suggests an interesting distribution of amino acids that may account for its helical structure and its ability to bind and transport lipid.

publication date

  • December 1974

Research

keywords

  • Academic Article

Identity

Language

  • eng

PubMed Central ID

  • PMC433829

PubMed ID

  • 4372630

Additional Document Info

start page

  • 3631

end page

  • 4

volume

  • 71

number

  • 9