Biomaterial Database

Amino acid sequence of human plasma apolipoprotein C-III from normolipidemic subjects. 1986

A V Hospattankar, and H B Brewer, and R Ronan, and T Fairwell

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.

UI	MeSH Term	Description	Entries
D006954	Hyperlipoproteinemia Type V	A severe type of hyperlipidemia, sometimes familial, that is characterized by the elevation of both plasma CHYLOMICRONS and TRIGLYCERIDES contained in VERY-LOW-DENSITY LIPOPROTEINS. Type V hyperlipoproteinemia is often associated with DIABETES MELLITUS and is not caused by reduced LIPOPROTEIN LIPASE activity as in HYPERLIPOPROTEINEMIA TYPE I .	Hyperchylomicronemia Late Onset,Hyperchylomicronemia With Hyperprebetalipoproteinemia, Familial,Hyperchylomicronemia, Late-Onset,Hyperlipemia, Combined Fat And Carbohydrate-Induced,Hyperlipemia, Mixed,Hyperlipidemia, Type V,Hyperlipoproteinemia Type 5,Hyperlipoproteinemia, Type V,Hyperchylomicronemia Late Onsets,Hyperchylomicronemia, Late Onset,Hyperchylomicronemias, Late-Onset,Hyperlipemia, Combined Fat And Carbohydrate Induced,Hyperlipemias, Mixed,Hyperlipidemias, Type V,Hyperlipoproteinemia Type 5s,Hyperlipoproteinemias, Type V,Late-Onset Hyperchylomicronemia,Late-Onset Hyperchylomicronemias,Mixed Hyperlipemia,Mixed Hyperlipemias,Type V Hyperlipidemia,Type V Hyperlipidemias,Type V Hyperlipoproteinemia,Type V Hyperlipoproteinemias
D010446	Peptide Fragments	Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.	Peptide Fragment,Fragment, Peptide,Fragments, Peptide
D002851	Chromatography, High Pressure Liquid	Liquid chromatographic techniques which feature high inlet pressures, high sensitivity, and high speed.	Chromatography, High Performance Liquid,Chromatography, High Speed Liquid,Chromatography, Liquid, High Pressure,HPLC,High Performance Liquid Chromatography,High-Performance Liquid Chromatography,UPLC,Ultra Performance Liquid Chromatography,Chromatography, High-Performance Liquid,High-Performance Liquid Chromatographies,Liquid Chromatography, High-Performance
D006801	Humans	Members of the species Homo sapiens.	Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000595	Amino Acid Sequence	The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.	Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D000596	Amino Acids	Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins.	Amino Acid,Acid, Amino,Acids, Amino
D001056	Apolipoproteins C	A group of apolipoproteins that can readily exchange among the various classes of lipoproteins (HDL; VLDL; CHYLOMICRONS). After lipolysis of TRIGLYCERIDES on VLDL and chylomicrons, Apo-C proteins are normally transferred to HDL. The subtypes can modulate remnant binding to receptors, LECITHIN CHOLESTEROL ACYLTRANSFERASE, or LIPOPROTEIN LIPASE.	Apo-C,Apo C,ApoC,Apoprotein (C),Apoproteins C
D014357	Trypsin	A serine endopeptidase that is formed from TRYPSINOGEN in the pancreas. It is converted into its active form by ENTEROPEPTIDASE in the small intestine. It catalyzes hydrolysis of the carboxyl group of either arginine or lysine. EC 3.4.21.4.	Tripcellim,Trypure,beta-Trypsin,beta Trypsin
D053305	Apolipoprotein C-III	A 9-kDa protein component of VERY-LOW-DENSITY LIPOPROTEINS and CHYLOMICRON REMNANTS. Apo C-III, synthesized in the liver, is an inhibitor of LIPOPROTEIN LIPASE. Apo C-III modulates the binding of chylomicron remnants and VLDL to receptors (RECEPTORS, LDL) thus decreases the uptake of triglyceride-rich particles by the liver cells and subsequent degradation. The normal Apo C-III is glycosylated. There are several polymorphic forms with varying amounts of SIALIC ACID (Apo C-III-0, Apo C-III-1, and Apo C-III-2).	Apo C-III,Apo C-III-2,ApoC-III,Apolipoprotein C-III-0,Apolipoprotein C-III-1,Apolipoprotein CIII,Sialyl Apo C-III,Sialyl Apolipoprotein C-III,Apo C III,Apo C III 2,Apo C-III, Sialyl,ApoC III,Apolipoprotein C III,Apolipoprotein C III 0,Apolipoprotein C III 1,Apolipoprotein C-III, Sialyl,Sialyl Apo C III,Sialyl Apolipoprotein C III