Abstract
Radiolabelled anhydrotrypsin was bound by alpha 2M (alpha 2-macroglobulin) sufficiently tightly to resist separation during gel electrophoresis; 2 mol of anhydrotrypsin were bound/mol of alpha 2M, but the interaction differed in important respects from that between active proteinases and alpha 2M. Anhydrotrypsin was bound by the electrophoretically 'fast' form of alpha 2M, although much less effectively than by the 'slow' form. The inactive enzyme was displaced from alpha 2M by trypsin inhibitor, the order of effectiveness being aprotinin > soya-bean trypsin inhibitor > benzamidine. Saturation of alpha 2M with anhydrotrypsin did not prevent subsequent binding and inhibition of active trypsin by the alpha 2M, and the anhydrotrypsin was not displaced during this reaction. Anhydrotrypsin bound by alpha 2M retained its ability to react with antibodies against trypsin, whereas bound trypsin did not.
Full text
PDF
Images in this article
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Ako H., Foster R. J., Ryan C. A. The preparation of anhydro-trypsin and its reactivity with naturally occurring proteinase inhibitors. Biochem Biophys Res Commun. 1972 Jun 28;47(6):1402–1407. doi: 10.1016/0006-291x(72)90228-8. [DOI] [PubMed] [Google Scholar]
- Axén R., Ernback S. Chemical fixation of enzymes to cyanogen halide activated polysaccharide carriers. Eur J Biochem. 1971 Feb 1;18(3):351–360. doi: 10.1111/j.1432-1033.1971.tb01250.x. [DOI] [PubMed] [Google Scholar]
- Barrett A. J., Brown M. A., Sayers C. A. The electrophoretically 'slow' and 'fast' forms of the alpha 2-macroglobulin molecule. Biochem J. 1979 Aug 1;181(2):401–418. doi: 10.1042/bj1810401. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Barrett A. J. Cathepsin D. Purification of isoenzymes from human and chicken liver. Biochem J. 1970 Apr;117(3):601–607. doi: 10.1042/bj1170601. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Barrett A. J. Chicken alpha2-proteinase inhibitor: a serum protein homologous with ovoinhibitor of egg white. Biochim Biophys Acta. 1974 Nov 5;371(1):52–62. doi: 10.1016/0005-2795(74)90154-8. [DOI] [PubMed] [Google Scholar]
- Barrett A. J., Starkey P. M. The interaction of alpha 2-macroglobulin with proteinases. Characteristics and specificity of the reaction, and a hypothesis concerning its molecular mechanism. Biochem J. 1973 Aug;133(4):709–724. doi: 10.1042/bj1330709. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Boyde T. R., Pryme I. F. Alpha2-macroglobulin binding of trypsin, chymotrypsin, papain, and cationic aspartate aminotransferase. Clin Chim Acta. 1968 Jul;21(1):9–14. doi: 10.1016/0009-8981(68)90003-x. [DOI] [PubMed] [Google Scholar]
- MARES-GUIA M., SHAW E. STUDIES ON THE ACTIVE CENTER OF TRYPSIN. THE BINDING OF AMIDINES AND GUANIDINES AS MODELS OF THE SUBSTRATE SIDE CHAIN. J Biol Chem. 1965 Apr;240:1579–1585. [PubMed] [Google Scholar]
- McPherson T. A., Marchalonis J. J., Lennon V. Binding of encephalitogenic basic protein by serum alpha-globulins. Immunology. 1970 Dec;19(6):929–933. [PMC free article] [PubMed] [Google Scholar]
- Stollar B. D., Rezuke W. Separation of anti-histone antibodies from nonimmune histone-precipitating serum proteins, predominantly alpha2-macroglobulin. Arch Biochem Biophys. 1978 Oct;190(2):398–404. doi: 10.1016/0003-9861(78)90292-8. [DOI] [PubMed] [Google Scholar]
- Tsuru D., Kado K., Fujiwara K., Tmimatsu M., Ogita K. Interaction of porcine alpha2-macroglobulin with chemically modified proteinases. J Biochem. 1978 May;83(5):1345–1353. doi: 10.1093/oxfordjournals.jbchem.a132042. [DOI] [PubMed] [Google Scholar]
- Vincent J. P., Lazdunski M. Trypsin-pancreatic trypsin inhibitor association. Dynamics of the interaction and role of disulfide bridges. Biochemistry. 1972 Aug 1;11(16):2967–2977. doi: 10.1021/bi00766a007. [DOI] [PubMed] [Google Scholar]