Abstract
Concanavalin A (con A) is a potent inhibitor of coagulant activity of native tissue factor. Coagulant activity is recovered by addition of alpha-methyl-D-glucoside to inhibited tissue factor. Inclusion of alpha-methyl-D-glucose during incubation of con A with tissue factor preserves coagulant activity. These data suggest that con A interacts reversibly with a carbohydrate residue in such a way as to inhibit coagulant activity of the molecule. Purified tissue factor apoprotein has been recombined with mixed brain phospholipids or purified phospholipids (phosphatidyl ethanolamine or a mixture of phosphatidyl choline with phosphatidyl serine). These preparations were also completely but reversibly inhibited by con A. Thus, purified tissue factor apoprotein appears to donate the affected carbohydrate residue.
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Selected References
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- Agrawal B. B., Goldstein I. J. Protein-carbohydrate interaction. VI. Isolation of concanavalin A by specific adsorption on cross-linked dextran gels. Biochim Biophys Acta. 1967 Oct 23;147(2):262–271. [PubMed] [Google Scholar]
- Burger M. M. A difference in the architecture of the surface membrane of normal and virally transformed cells. Proc Natl Acad Sci U S A. 1969 Mar;62(3):994–1001. doi: 10.1073/pnas.62.3.994. [DOI] [PMC free article] [PubMed] [Google Scholar]
- GOLDSTEIN I. J., HOLLERMAN C. E., MERRICK J. M. PROTEIN-CARBOHYDRATE INTERACTION. I. THE INTERACTION OF POLYSACCHARIDES WITH CONCANAVALIN A. Biochim Biophys Acta. 1965 Jan 4;97:68–76. doi: 10.1016/0304-4165(65)90270-9. [DOI] [PubMed] [Google Scholar]
- GOLDSTEIN I. J., HOLLERMAN C. E., SMITH E. E. PROTEIN-CARBOHYDRATE INTERACTION. II. INHIBITION STUDIES ON THE INTERACTION OF CONCANAVALIN A WITH POLYSACCHARIDES. Biochemistry. 1965 May;4:876–883. doi: 10.1021/bi00881a013. [DOI] [PubMed] [Google Scholar]
- Inbar M., Sachs L. Interaction of the carbohydrate-binding protein concanavalin A with normal and transformed cells. Proc Natl Acad Sci U S A. 1969 Aug;63(4):1418–1425. doi: 10.1073/pnas.63.4.1418. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Jesty J., Nemerson Y. Purification of Factor VII from bovine plasma. Reaction with tissue factor and activation of Factor X. J Biol Chem. 1974 Jan 25;249(2):509–515. [PubMed] [Google Scholar]
- Kalb A. J., Lustig A. The molecular weight of concanavalin A. Biochim Biophys Acta. 1968 Oct 21;168(2):366–367. doi: 10.1016/0005-2795(68)90161-x. [DOI] [PubMed] [Google Scholar]
- LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
- Li S. C., Li Y. T. Studies on the glycosidases of jack bean meal. 3. Crystallization and properties of beta-N-acetylhexosaminidase. J Biol Chem. 1970 Oct 10;245(19):5153–5160. [PubMed] [Google Scholar]
- Li Y. T. Studies on the glycosidases in jack bean meal. I. Isolation and properties of alpha-mannosidase. J Biol Chem. 1967 Dec 10;242(23):5474–5480. [PubMed] [Google Scholar]
- Nemerson Y. Characteristics and lipid requirements of coagulant proteins extracted from lung and brain: the specifity of protein component of tissue factor. J Clin Invest. 1969 Feb;48(2):322–331. doi: 10.1172/JCI105988. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Nemerson Y., Clyne L. P. An assay for coagulation factor VII using factor VII-depleted bovine plasma. J Lab Clin Med. 1974 Feb;83(2):301–303. [PubMed] [Google Scholar]
- Nemerson Y., Esnouf M. P. Activation of a proteolytic system by a membrane lipoprotein: mechanism of action of tissue factor. Proc Natl Acad Sci U S A. 1973 Feb;70(2):310–314. doi: 10.1073/pnas.70.2.310. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Nemerson Y., Pitlick F. A. Purification and characterization of the protein component of tissue factor. Biochemistry. 1970 Dec 22;9(26):5100–5105. doi: 10.1021/bi00828a009. [DOI] [PubMed] [Google Scholar]
- Nemerson Y. The phospholipid requirement of tissue factor in blood coagulation. J Clin Invest. 1968 Jan;47(1):72–80. doi: 10.1172/JCI105716. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Nemerson Y. The reaction between bovine brain tissue factor and factors VII and X. Biochemistry. 1966 Feb;5(2):601–608. doi: 10.1021/bi00866a029. [DOI] [PubMed] [Google Scholar]
- Olson M. O., Liener I. E. The association and dissociation of concanavalin A, the phytohemagglutinin of the jack bean. Biochemistry. 1967 Dec;6(12):3801–3808. doi: 10.1021/bi00864a025. [DOI] [PubMed] [Google Scholar]
- Osterud B., Berre A., Otnaess A. B., Bjorklid E., Prydz H. Activation of the coagulation factor VII by tissue thromboplastin and calcium. Biochemistry. 1972 Jul 18;11(15):2853–2857. doi: 10.1021/bi00765a018. [DOI] [PubMed] [Google Scholar]
- Rickles F. R., Hardin J. A., Pitlick F. A., Hoyer L. W., Conrad M. E. Tissue factor activity in lymphocyte cultures from normal individuals and patients with hemophilia A. J Clin Invest. 1973 Jun;52(6):1427–1434. doi: 10.1172/JCI107316. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Steinemann A., Stryer L. Accessibility of the carbohydrate moiety of rhodopsin. Biochemistry. 1973 Apr 10;12(8):1499–1502. doi: 10.1021/bi00732a005. [DOI] [PubMed] [Google Scholar]
- Sumner J. B., Howell S. F. Identification of Hemagglutinin of Jack Bean with Concanavalin A. J Bacteriol. 1936 Aug;32(2):227–237. doi: 10.1128/jb.32.2.227-237.1936. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Sumner J. B., Howell S. F., Zeissig A. CONCANAVALIN A AND HEMAGGLUTINATION. Science. 1935 Jul 19;82(2116):65–66. doi: 10.1126/science.82.2116.65. [DOI] [PubMed] [Google Scholar]
- Wang J. L., Cunningham B. A., Edelman G. M. Unusual fragments in the subunit structure of concanavalin A. Proc Natl Acad Sci U S A. 1971 Jun;68(6):1130–1134. doi: 10.1073/pnas.68.6.1130. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Zeldis S. M., Nemerson Y., Pitlick F. A., Lentz T. L. Tissue factor (thromboplastin): localization to plasma membranes by peroxidase-conjugated antibodies. Science. 1972 Feb 18;175(4023):766–768. doi: 10.1126/science.175.4023.766. [DOI] [PubMed] [Google Scholar]