Characterization of human, bovine, and horse antithrombin III.
Abstract: A comparison of the physical-chemical properties of human, bovine, and horse antithrombin III has been made. These three plasma proteins are strong inhibitors of bovine factor Xa and form a 1:1 molar complex with this coagulation enzyme. Human, bovine, and horse antithrombin III are glycoproteins containing hexose, hexosamine, and neuraminic acid. The total carbohydrate was 9, 12, and 16% for human, bovine, and horse antithrombin III, respectively. These proteins have a similar amino acid composition, although some monor variations were noted. Each antithrombin III is composed of a single polypeptide chain with an amino-terminal histidine residue. Of the first 17 amino-terminal residues, only three differences were noted between the three proteins. These occur in position 2 which is occupied by Gly, Arg, and Trp in human, bovine, and horse, respectively; position 6 which has a deletion in human antithrombin III; and position 8 where Ile in human and horse antithrombin III has been replaced by Val in the bovine preparation. The remainder of the first 17 residues is the same in all three proteins. The molecular weights for the bovine and horse preparation were 56 600 and 52 500, respectively, as determined by sedimentation equilibrium in the presence of guanidine hydrochloride. Some immunological cross-reactivity was also observed between the three different proteins.
Publication Date: 1976-01-27 PubMed ID: 1247522DOI: 10.1021/bi00647a020Google Scholar: Lookup
The Equine Research Bank provides access to a large database of publicly available scientific literature. Inclusion in the Research Bank does not imply endorsement of study methods or findings by Mad Barn.
- Journal Article
- Research Support
- U.S. Gov't
- P.H.S.
Summary
This research summary has been generated with artificial intelligence and may contain errors and omissions. Refer to the original study to confirm details provided. Submit correction.
This study compares the physical and chemical properties of antithrombin III, a plasma protein found in humans, bovines, and horses, which plays an essential role in blood coagulation. The researchers observe differences in carbohydrate content and some slight variations in amino acid composition between the three variants, and note some minor cross-reactivity between them in immunological tests.
Physical-Chemical Comparison of Antithrombin III
- The researchers compared the physical-chemical properties of human, bovine (cow), and horse antithrombin III, plasma proteins which act as strong inhibitors of the enzyme bovine factor Xa, which is involved in blood coagulation.
- All three proteins are glycoproteins, meaning they contain carbohydrates connected to proteins. These carbohydrates include hexose, hexosamine, and neuraminic acid (also known as sialic acid).
- The total carbohydrate content varies between the three proteins: 9% in humans, 12% in bovines, and 16% in horses.
Amino Acid Structure of Antithrombin III
- Each antithrombin III protein is made up of a single chain of amino acids with an amino-terminal (starting) histidine residue, which is a specific type of amino acid.
- All three proteins have a similar amino acid structure, but minor variations were detected. These variations occur in positions 2, 6, and 8 of the amino acid sequence.
- Position 2 is occupied by glycine (Gly) in humans, arginine (Arg) in bovines, and tryptophan (Trp) in horses.
- Position 6 features a deletion in the human version of antithrombin III, meaning this position doesn’t exist in the human protein sequence.
- At position 8, isoleucine (Ile) in human and horse antithrombin III is replaced by valine (Val) in the bovine version.
- Despite these variations, the remainder of the first 17 residues in the amino acid sequence was identical in all three proteins.
Molecular Weights and Immunological Cross-Reactivity
- The researchers measured the molecular weights of the bovine and horse versions of the protein, finding them to be 56,600 and 52,500, respectively, when measured in the presence of guanidine hydrochloride, a strong denaturant.
- Some immunological cross-reactivity was observed between the three proteins, indicating that the immune systems of each species would recognize the proteins from the other species to some degree.
Cite This Article
APA
Kurachi K, Schmer G, Hermodson MA, Teller DC, Davie EW.
(1976).
Characterization of human, bovine, and horse antithrombin III.
Biochemistry, 15(2), 368-373.
https://doi.org/10.1021/bi00647a020 Publication
Researcher Affiliations
MeSH Terms
- Amino Acids / analysis
- Animals
- Antithrombins / analysis
- Antithrombins / pharmacology
- Blood Coagulation Tests
- Cattle
- Enzyme Activation / drug effects
- Factor X / metabolism
- Horses
- Humans
- Immunoelectrophoresis
- Molecular Weight
- Species Specificity
Citations
This article has been cited 18 times.- Piepkorn MW. Dansyl (5-dimethylaminonaphthalene-1-sulphonyl)-heparin binds antithrombin III and platelet factor 4 at separate sites. Biochem J 1981 May 15;196(2):649-51.
- DiScipio RG. The activation of the alternative pathway C3 convertase by human plasma kallikrein. Immunology 1982 Mar;45(3):587-95.
- Björk I, Lindahl U. Mechanism of the anticoagulant action of heparin. Mol Cell Biochem 1982 Oct 29;48(3):161-82.
- Bock SC, Wion KL, Vehar GA, Lawn RM. Cloning and expression of the cDNA for human antithrombin III. Nucleic Acids Res 1982 Dec 20;10(24):8113-25.
- Lollar P, Owen WG. Clearance of thrombin from circulation in rabbits by high-affinity binding sites on endothelium. Possible role in the inactivation of thrombin by antithrombin III. J Clin Invest 1980 Dec;66(6):1222-30.
- Fuchs HE, Trapp HG, Griffith MJ, Roberts HR, Pizzo SV. Regulation of factor IXa in vitro in human and mouse plasma and in vivo in the mouse. Role of the endothelium and the plasma proteinase inhibitors. J Clin Invest 1984 Jun;73(6):1696-703.
- Fuchs HE, Pizzo SV. Regulation of factor Xa in vitro in human and mouse plasma and in vivo in mouse. Role of the endothelium and plasma proteinase inhibitors. J Clin Invest 1983 Dec;72(6):2041-9.
- Tollefsen DM, Blank MK. Detection of a new heparin-dependent inhibitor of thrombin in human plasma. J Clin Invest 1981 Sep;68(3):589-96.
- Carlson TH, Atencio AC, Simon TL. Comparison of the behaviour in vivo of two molecular forms of antithrombin III. Biochem J 1985 Feb 1;225(3):557-64.
- Tollefsen DM, Pestka CA. Modulation of heparin cofactor II activity by histidine-rich glycoprotein and platelet factor 4. J Clin Invest 1985 Feb;75(2):496-501.
- Patterson SD, Bell K. The equine protease inhibitory system (Pi): abnormal expressions of PiF, PiL, and PiS1. Biochem Genet 1986 Aug;24(7-8):529-43.
- Barrowcliffe TW, Havercroft SJ, Kemball-Cook G, Lindahl U. The effect of Ca2+, phospholipid and factor V on the anti-(factor Xa) activity of heparin and its high-affinity oligosaccharides. Biochem J 1987 Apr 1;243(1):31-7.
- Jane SM, Mitchell CA, Hau L, Salem HH. Inhibition of activated protein C by platelets. J Clin Invest 1989 Jan;83(1):222-6.
- Mejdoub H, Le Ret M, Boulanger Y, Maman M, Choay J, Reinbolt J. The complete amino acid sequence of bovine antithrombin (ATIII). J Protein Chem 1991 Apr;10(2):205-12.
- Bell K, Arthur H, van Oorschot RA, VandeBerg JL. Antithrombin III (AT3) polymorphism in the marsupial Monodelphis domestica: identification and genetics. Biochem Genet 1992 Dec;30(11-12):591-601.
- Shuman MA, Majerus PW. The measurement of thrombin in clotting blood by radioimmunoassay. J Clin Invest 1976 Nov;58(5):1249-58.
- Di Scipio RG, Kurachi K, Davie EW. Activation of human factor IX (Christmas factor). J Clin Invest 1978 Jun;61(6):1528-38.
- Kisiel W. Human plasma protein C: isolation, characterization, and mechanism of activation by alpha-thrombin. J Clin Invest 1979 Sep;64(3):761-9.
Use Nutrition Calculator
Check if your horse's diet meets their nutrition requirements with our easy-to-use tool Check your horse's diet with our easy-to-use tool
Talk to a Nutritionist
Discuss your horse's feeding plan with our experts over a free phone consultation Discuss your horse's diet over a phone consultation
Submit Diet Evaluation
Get a customized feeding plan for your horse formulated by our equine nutritionists Get a custom feeding plan formulated by our nutritionists
