1986/03/03 by Ashok Hospattankar, H Bryan Brewer, Rosemary Ronan +1 · 1 citation
Chemistry · Medicine · #Amino acid #Apolipoprotein B #Biochemistry #Blood Coagulation and Thrombosis Mechanisms #Chemistry #Cholesterol #Chromatography #Diabetes, Cardiovascular Risks, and Lipoproteins #Digestion (alchemy) #Edman degradation #Gene #Lipoproteins and Cardiovascular Health #Mass spectrometry #Peptide sequence #Protein primary structure #Protein sequencing #Sequence (biology)
paper · doi:10.1016/0014-5793(86)80300-3
openalex publication_date 1986/03/03 · openalex created_date 2016/06/24 · openalex updated_date 2026/07/22
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 normolipidemic 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.