MHC Class III products: an electron microscopic study of the C3 convertases of human complement.
J Exp Med
; 159(1): 324-9, 1984 Jan 01.
Article
em En
| MEDLINE
| ID: mdl-6559206
ABSTRACT
We have reported a transmission electron microscopic study of the two C3 convertases of human complement and their precursors. The corresponding proteins and complexes of the classical and alternative pathway appear very similar. Cofactors C3b and C4b are nearly indistinguishable and display a characteristic but highly irregular substructure. C2 and Factor B are globular with diameters of 85 +/- 8 A and 80 +/- 8 A and both consist of three discrete globular domains each approximately 40 A in diameter. Bb and C2a each contain two domains connected by a short linker segment. Both domains of Bb and one domain of C2a are 42 A in diameter (28 kd), while the second domain of C2 is 47 A in diameter (39 kd). Attachment of the enzymatic subunits to cofactors occurs through one domain only.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Biossíntese de Proteínas
/
Enzimas Ativadoras do Complemento
/
Convertases de Complemento C3-C5
/
Complexo Principal de Histocompatibilidade
Limite:
Humans
Idioma:
En
Revista:
J Exp Med
Ano de publicação:
1984
Tipo de documento:
Article