Effects of manganese and calcium on conformational stability of concanavalin A: A differential scanning calorimetric study
作者： James C. Zahnley
DOI: 10.1016/S0162-0134(00)80136-1
关键词:
摘要: The effect of degree saturation concanavalin A with Mn2+ or Ca2+, both, on its thermal denaturation was investigated by differential scanning calorimetry. Acid-demetallized partly fully remetallized in acetate buffer (pH 5.0) containing 0.4 to 0.5 M NaCl. Under these conditions, native dimeric is highly stable, undergoing heat at 101 degrees C, an enthalpy 7.4 cal/g. Removal metal ions lowered stability considerably; 0.06 Mn2+/monomer and 0.23 Ca2+/monomer (mol/mol) denatured 74 C 3.2 Added stabilized demetallized A, but added Ca2+ alone (up 2 mol/mol monomer) did not. Ca2+/ ratio influenced stabilization Mn2+. In the presence 1 Mn2+/ monomer less (mol/mol), 85-88 94-97 degress indicating two metallo-concanavalin species. At 1.0 more mole each per monomer, one endotherm observed above 98 increased 5.3 cal/g from than 3.6 lower ion/protein ratios. Stabilization greater plus alone, consistent intrasubunit cooperativity ion-induced A.
elsevier.com
sci-hub.se 参考文章(44)
A.D. Cardin, W.D. Behnke, F. Mandel, Time-dependent changes in the intrinsic cotton effects of concanavalin A. Journal of Biological Chemistry. ,vol. 254, pp. 8877- 8884 ,(1979) , 10.1016/S0021-9258(19)86781-9
Irwin J. Goldstein, Colleen E. Hayes, The lectins : carbohydrate-binding proteins of plants and animals Advances in Carbohydrate Chemistry and Biochemistry. ,vol. 35, pp. 127- 340 ,(1978) , 10.1016/S0065-2318(08)60220-6
Joseph J. Villafranca, Ronald E. Viola, Proton nuclear magnetic resonance studies of the manganese (II) binding site of concanavalin A Archives of Biochemistry and Biophysics. ,vol. 165, pp. 51- 59 ,(1974) , 10.1016/0003-9861(74)90140-4
J J Grimaldi, B D Sykes, Concanavalin A: a stopped flow nuclear magnetic resonance study of conformational changes induced by Mn++, Ca++, and alpha-methyl-D-mannoside. Journal of Biological Chemistry. ,vol. 250, pp. 1618- 1624 ,(1975) , 10.1016/S0021-9258(19)41738-9
Menahem Shoham, Ada Yonath, Joel L. Sussman, John Moult, Wolfie Traub, A.Joseph Kalb (Gilboa), Crystal structure of demetallized concanavalin A: the metal-binding region. Journal of Molecular Biology. ,vol. 131, pp. 137- 155 ,(1979) , 10.1016/0022-2836(79)90070-6
Brian H. Barber, Jeremy P. Carver, Magnetic Resonance Studies of Concanavalin A: Conformational Changes Induced by Ca2+ and α-Methyl-D-mannopyranoside Biochemistry and Cell Biology. ,vol. 53, pp. 371- 379 ,(1975) , 10.1139/O75-051
G. N. Reeke, J. W. Becker, G. M. Edelman, Changes in the three-dimensional structure of concanavalin A upon demetallization Proceedings of the National Academy of Sciences of the United States of America. ,vol. 75, pp. 2286- 2290 ,(1978) , 10.1073/PNAS.75.5.2286
Menahem Shoham, Joel L. Sussman, Ada Yonath, John Moult, Wolfie Traub, A.Joseph KalbGilboa, The effect of binding of metal ions on the three-dimensional structure of demetallized concanavalin A FEBS Letters. ,vol. 95, pp. 54- 56 ,(1978) , 10.1016/0014-5793(78)80050-7
J. W. BECKER, G. N. REEKE, B. A. CUNNINGHAM, G. M. EDELMAN, New evidence on the location of the saccharide-binding site of concanavalin A. Nature. ,vol. 259, pp. 406- 409 ,(1976) , 10.1038/259406A0
Gerald M. Alter, James A. Magnuson, Kinetic study of manganese association to demetallized concanavalin A. Biochemistry. ,vol. 18, pp. 29- 36 ,(1979) , 10.1021/BI00568A005