skip to main content
Idioma:

The Enzymatic Measurement of Binding of First Component of Guinea Pig Complement with Formalized Sheep Erythrocytes Sensitized with Rabbit Antiserum

MORI, Yoki ; KAWAI, Nobukazu ; KOYAMA, Jiro

Journal of biochemistry (Tokyo), 1973-05, Vol.73 (5), p.951-958 [Periódico revisado por pares]

England: Oxford University Press

Texto completo disponível

Citações Citado por
  • Título:
    The Enzymatic Measurement of Binding of First Component of Guinea Pig Complement with Formalized Sheep Erythrocytes Sensitized with Rabbit Antiserum
  • Autor: MORI, Yoki ; KAWAI, Nobukazu ; KOYAMA, Jiro
  • Assuntos: Animals ; Antigen-Antibody Complex ; Binding Sites ; Calcium ; Complement Inactivator Proteins ; Complement System Proteins ; Erythrocytes - immunology ; Esters ; Formaldehyde ; Guinea Pigs - immunology ; Hydrolysis ; Immune Sera ; Protein Binding ; Rabbits - immunology ; Sheep - immunology
  • É parte de: Journal of biochemistry (Tokyo), 1973-05, Vol.73 (5), p.951-958
  • Notas: ark:/67375/HXZ-CK8QXSGN-P
    ArticleID:73.5.951
    istex:2AFDA7A76D0DBD0057619EB819964960D7D04F5D
    ObjectType-Article-1
    SourceType-Scholarly Journals-1
    ObjectType-Feature-2
    content type line 23
  • Descrição: The enzymatic measurement of binding of first component (C1)* of guinea pig complement with antigen-antibody complexes is described. The reaction was based on the abilities of this component to bind with formalized sheep erythrocytes (FSE) sensitized with rabbit antiserum to sheep erythrocytes (SE) and to hydrolyze N-acetyl-L-tyrosine ethyl ester (ATEE). When sensitized FSE were incubated with guinea pig serum or partially purified CĪ at 0°C and washed with an appropriate buffer, these materials showed esterolytic activity. This activity increased proportionally to the amount of rabbit antibody used for sensitization. When guinea pig serum was used as a source of Cl and the binding reaction was carried out at 37°C, no CĪ activity developed, due to the coexistence of CĪ inactivator. This blocked the esterolytic activity of CĪs at 37°C immediately after the activation of Cls to Cls. As the binding of Cl with sensitized FSE proceeded rapidly and also quantitatively at 0°C, this reaction could be used for the enzymatic determination of Cl activity, independently of whether preparations of Cl to be tested contained CI¯ inactivator or not.
  • Editor: England: Oxford University Press
  • Idioma: Inglês
Links
Voltar para lista de resultados

  • Realização: ABCD-USP USP   Logos de Redes Sociais: Freepik

Buscando em bases de dados remotas. Favor aguardar.