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1.
In. Palomo González, Iván; Ferreira Vigoroux, Arturo; Sepúlveda Carvajal, Cecilia; Rosemblatt Silber, Mario; Vergara Castillo, Ulises. Fundamentos de inmunología. Talca, Universidad de Talca, 1998. p.319-49, ilus, tab.
Monografia em Espanhol | LILACS | ID: lil-284814
3.
FEBS Lett ; 269(1): 19-22, 1990 Aug 20.
Artigo em Inglês | MEDLINE | ID: mdl-2143735

RESUMO

The catalytic domains of activated C1r and C1s, comprising the C-terminal region of the A chain (gamma), disulphide-linked to the B chain, were obtained by limited proteolysis of the native proteases with chymotrypsin and plasmin, respectively, and studied by small angle neutron scattering. For activated C1s (gamma-B), a molar mass of 45,000 +/- 5000 g/mol, and a relatively large radius of gyration (Rg) of 28 +/- 1 A were determined, excluding a single globular domain. The corresponding values for activated C1r (gamma-B)2 (90,000 g/mol, Rg = 34 +/- 1 A) are consistent with a dimer involving the loose packing of two (gamma-B) subunits. Various models of the dimer are discussed in the light of neutron scattering and other data.


Assuntos
Complemento C1r/ultraestrutura , Complemento C1s/ultraestrutura , Quimotripsina/farmacologia , Ativação Enzimática , Fibrinolisina/farmacologia , Humanos , Técnicas In Vitro , Peso Molecular , Nêutrons , Conformação Proteica , Espalhamento de Radiação , Serina Endopeptidases , Solventes
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