The α2 macroglobulin/thrombin interaction in the presence of hydroxylamine
作者： P. Lambin , F. Pochon , J.M. Fine , M. Steinbuch
DOI: 10.1016/0049-3848(83)90024-5
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摘要: Abstract The influence of a primary amine, hydroxylamine, on the interaction between α 2 macroglobulin ( M) and thrombin was analyzed by electrophoretic enzymatic methods. Hydroxylamine (final concentrations 0.01 M 0.1 added to solution 3 5 min before thrombin. In these conditions hydroxylamine had no direct itself. inhibition activity still possible M/thrombin complexes were observed. However rate clotting diminished in function concentration. obtained absence nucleophylic agent resistant SDS dissociation, whereas those presence dissociated SDS. both cases, amount polypeptide chains cleaved same (50%). conclusion, does not prevent formation complexes, but it reduces covalent binding enzyme inhibitor concentration dependant fashion, leading “abnormal” complexes.
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sci-hub.se 参考文章(19)
R M Topping, A H Craven, The identification of distinctive forms of human α2-macroglobulin by using the numerical relationship between trypsin binding in α- and β-modes Biochemical Journal. ,vol. 177, pp. 501- 508 ,(1979) , 10.1042/BJ1770501
Lars Sottrup-Jensen, Torben E. Petersen, Staffan Magnusson, Mechanism of proteinase complex formation with α2-macroglobulin: Three modes of trypsin binding FEBS Letters. ,vol. 128, pp. 127- 132 ,(1981) , 10.1016/0014-5793(81)81097-6
Lars Sottrup-Jensen, Peter B. Lønblad, Terrence M. Stepanik, Torben E. Petersen, Staffan Magnusson, Hans Jörnvall, Primary structure of the ‘bait’ region for proteinases in α2-macroglobulin: Nature of the complex FEBS Letters. ,vol. 127, pp. 167- 173 ,(1981) , 10.1016/0014-5793(81)80197-4
J.G. Bieth, M. Tourbez-Perrin, F. Pochon, Inhibition of alpha 2-macroglobulin-bound trypsin by soybean trypsin inhibitor. Journal of Biological Chemistry. ,vol. 256, pp. 7954- 7957 ,(1981) , 10.1016/S0021-9258(18)43372-8
K. Wu, D. Wang, R.D. Feinman, Inhibition of proteases by alpha 2-macroglobulin. The role of lysyl amino groups of trypsin in covalent complex formation. Journal of Biological Chemistry. ,vol. 256, pp. 10409- 10414 ,(1981) , 10.1016/S0021-9258(19)68634-5
G S Salvesen, A J Barrett, Covalent binding of proteinases in their reaction with α2-macroglobulin Biochemical Journal. ,vol. 187, pp. 695- 701 ,(1980) , 10.1042/BJ1870695
F Van Leuven, J J Cassiman, H Van den Berghe, Functional modifications of alpha 2-macroglobulin by primary amines. I. Characterization of alpha 2 M after derivatization by methylamine and by factor XIII Journal of Biological Chemistry. ,vol. 256, pp. 9016- 9022 ,(1981) , 10.1016/S0021-9258(19)52501-7
H.G.J. Brummelhuis, J. Over, C.C. Duivis-Vorst, L.A. Wilson-de Stürler, G. Ates, P.J. Hoek, E.E. Reerink-Brongers, Contributions to the Optimal Use of Human Blood Vox Sanguinis. ,vol. 45, pp. 205- 216 ,(1974) , 10.1111/J.1423-0410.1983.TB01906.X
M. Steinbuch, L. Pejaudier, M. Quentin, V. Martin, Molecular alteration of α2-macroglobulin by aliphatic amines Biochimica et Biophysica Acta. ,vol. 154, pp. 228- 231 ,(1968) , 10.1016/0005-2795(68)90277-8
Lars Sottrup-Jensen, Torben E. Petersen, Staffan Magnusson, Trypsin-induced activation of the thiol esters in α2-macroglobulin generates a short-lived intermediate (‘nascent’ α2M) that can react rapidly to incorporate not only methylamine or putrescine but also proteins lacking proteinase activity FEBS Letters. ,vol. 128, pp. 123- 126 ,(1981) , 10.1016/0014-5793(81)81096-4