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Amino acid sequence of human plasma apolipoprotein C‐III from normalipidemic subjects
Author(s) -
Hospattankar Ashok V.,
Bryan Brewer H.,
Ronan Rosemary,
Fairwell Thomas
Publication year - 1986
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(86)80300-3
Subject(s) - edman degradation , peptide sequence , amino acid , chemistry , biochemistry , apolipoprotein b , protein primary structure , protein sequencing , digestion (alchemy) , mass spectrometry , chromatography , sequence (biology) , gene , cholesterol
The complete amino acid sequence of human plasma apolipoprotein C‐III (apoC‐III) isolated from normal subjects is described. ApoC‐III is a linear polypeptide chain of 79 amino acids. Tryptic digestion of intact apoC‐III produced 5 major peptides, while tryptic digestion of the citraconylated protein yielded two peptides. The complete amino acid sequence of apoC‐III was determined by the automated Edman degradation of the intact protein as well as the various tryptic peptides. Phenylthiohydantoin amino acids were identified by high‐performance liquid chromatography and chemical ionization mass spectrometry. The amino acid sequence of apoC‐III isolated from normalipidemic subjects is identical to the apoC‐III sequence derived from the cDNA sequence and differs at 4 positions from the previously reported sequence of apoC‐III derived from a patient with type V hyperlipoproteinemia.