Comparative studies on thermodynamic characteristics of pea legumin and legumin-T thermal denaturation.
Int J Biol Macromol
; 29(4-5): 225-36, 2001 Dec 10.
Article
en En
| MEDLINE
| ID: mdl-11718818
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 alpha- and beta-polypeptide chains. The analysis of experimental data based on some assumptions showed that the splitting of C-termini of alpha-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 alpha-chains, as well as decrease of the temperatures of their maximum stability.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Proteínas de Plantas
Idioma:
En
Revista:
Int J Biol Macromol
Año:
2001
Tipo del documento:
Article
País de afiliación:
Rusia
Pais de publicación:
Países Bajos