Comparative studies on thermodynamic characteristics of pea legumin and legumin-T thermal denaturation |
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Authors: | G O Kozhevnikov A N Danilenko E E Braudo K D Schwenke |
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Institution: | a Russian Academy of Sciences, N.M. Emanuel Institute of Biochemical Physics, 4 Kosygin St., Moscow 119991, Russia b Institute of Applied Protein Chemistry, Kleimachnow, Germany |
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Abstract: | Characteristics of thermal denaturation of pea legumin and a product of its limited proteolysis with trypsin – legumin-T, in a wide range of NaCl concentrations have bean measured by means of differential scanning microcalorimetry. By the increase of NaCl concentration, the number of cooperative units (domains) increases from 1 per one polypeptide chain to 2 for legumin and 1.8 for legumin-T. Deconvolution of denaturation peaks have revealed up to three peaks, which were ascribed to the dissociation of protein macromolecules to subunits and the unfolding of - and β-polypeptide chains. The analysis of experimental data based on some assumptions showed that the splitting of C-termini of -chains, which are not constituents of cooperative domains, in the course of limited trypsinolysis results in destabilization of the quaternary structure of legumin and loosening of -chains, as well as decrease of the temperatures of their maximum stability. |
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Keywords: | Pea legumin Legumin-T Thermal denaturation |
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