BIOMAT Database Logo BIOMAT Database Logo

Scission of human apolipoprotein B-100 by kallikrein: characterization of the cleavage site. 1986

D A Hardman, and A Gustafson, and J W Schilling, and V H Donaldson, and J P Kane

Low density lipoprotein (LDL) from human plasma was digested with the specific endoprotease, kallikrein. Apolipoprotein B-100, the protein moiety of LDL, was cleaved by kallikrein into two fragments (K1 and K2) which we have compared to the naturally occurring fragments, B-74 and B-26. We have found that K1 and K2 precisely match B-74 and B-26 with respect to molecular weight, stoichiometry, and amino terminal amino acid sequence. These findings provide strong evidence that kallikrein is the agent responsible for the formation of B-74 and B-26 in human LDL.

UI MeSH Term Description Entries
D007610 Kallikreins Proteolytic enzymes from the serine endopeptidase family found in normal blood and urine. Specifically, Kallikreins are potent vasodilators and hypotensives and increase vascular permeability and affect smooth muscle. They act as infertility agents in men. Three forms are recognized, PLASMA KALLIKREIN (EC 3.4.21.34), TISSUE KALLIKREIN (EC 3.4.21.35), and PROSTATE-SPECIFIC ANTIGEN (EC 3.4.21.77). Kallikrein,Kininogenase,Callicrein,Dilminal,Kallidinogenase,Kalliginogenase,Kallikrein A,Kallikrein B',Kallikrein Light Chain,Kinin-Forming Enzyme,Padutin,alpha-Kallikrein,beta-Kallikrein,beta-Kallikrein B,Enzyme, Kinin-Forming,Kinin Forming Enzyme,Light Chain, Kallikrein,alpha Kallikrein,beta Kallikrein,beta Kallikrein B
D010446 Peptide Fragments Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques. Peptide Fragment,Fragment, Peptide,Fragments, Peptide
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
D001055 Apolipoproteins B Major structural proteins of triacylglycerol-rich LIPOPROTEINS. There are two forms, apolipoprotein B-100 and apolipoprotein B-48, both derived from a single gene. ApoB-100 expressed in the liver is found in low-density lipoproteins (LIPOPROTEINS, LDL; LIPOPROTEINS, VLDL). ApoB-48 expressed in the intestine is found in CHYLOMICRONS. They are important in the biosynthesis, transport, and metabolism of triacylglycerol-rich lipoproteins. Plasma Apo-B levels are high in atherosclerotic patients but non-detectable in ABETALIPOPROTEINEMIA. Apo-B,Apo B,ApoB,Apoprotein (B),Apoproteins B
D001665 Binding Sites The parts of a macromolecule that directly participate in its specific combination with another molecule. Combining Site,Binding Site,Combining Sites,Site, Binding,Site, Combining,Sites, Binding,Sites, Combining
D053299 Apolipoprotein B-100 A 513-kDa protein synthesized in the LIVER. It serves as the major structural protein of low-density lipoproteins (LIPOPROTEINS, LDL; LIPOPROTEINS, VLDL). It is the ligand for the LDL receptor (RECEPTORS, LDL) that promotes cellular binding and internalization of LDL particles. Apo B-100,Apo-B-100,ApoB-100,Apo B 100,ApoB 100,Apolipoprotein B 100

Related Publications

D A Hardman, and A Gustafson, and J W Schilling, and V H Donaldson, and J P Kane
Determinants of kallikrein proteolysis of apolipoprotein B-100 in human blood plasma.
February 1988, European journal of clinical investigation,
D A Hardman, and A Gustafson, and J W Schilling, and V H Donaldson, and J P Kane
Degradation of human apolipoprotein B-100 by apolipoprotein(a).
December 1993, FEBS letters,
D A Hardman, and A Gustafson, and J W Schilling, and V H Donaldson, and J P Kane
Thrombin cleavage of apolipoprotein Bh of rabbit LDL: structural comparisons with human apolipoprotein B-100.
June 1992, Journal of lipid research,
D A Hardman, and A Gustafson, and J W Schilling, and V H Donaldson, and J P Kane
Isolation and characterization of apolipoprotein B-100.
January 1986, Methods in enzymology,
D A Hardman, and A Gustafson, and J W Schilling, and V H Donaldson, and J P Kane
Characterization and quantitation of apolipoprotein B-100 by capillary electrophoresis.
January 1998, Journal of lipid research,
D A Hardman, and A Gustafson, and J W Schilling, and V H Donaldson, and J P Kane
Human apolipoprotein B-100 heparin-binding sites.
August 1987, The Journal of biological chemistry,
D A Hardman, and A Gustafson, and J W Schilling, and V H Donaldson, and J P Kane
Isolation and characterization of sulfhydryl and disulfide peptides of human apolipoprotein B-100.
July 1990, Proceedings of the National Academy of Sciences of the United States of America,
D A Hardman, and A Gustafson, and J W Schilling, and V H Donaldson, and J P Kane
The N-terminal domain of apolipoprotein B-100: structural characterization by homology modeling.
July 2007, BMC biochemistry,
D A Hardman, and A Gustafson, and J W Schilling, and V H Donaldson, and J P Kane
Isolation, expression and characterization of a human apolipoprotein B 100-specific cDNA clone.
October 1986, Biological chemistry Hoppe-Seyler,
D A Hardman, and A Gustafson, and J W Schilling, and V H Donaldson, and J P Kane
Degradation of apolipoprotein B-100 in human chylomicrons.
May 1988, Biochimica et biophysica acta,
Copied contents to your clipboard!