Zobrazeno 1 - 8
of 8
pro vyhledávání: '"W J, Monafo"'
Publikováno v:
Journal of Biological Chemistry. 261:8854-8858
Heparin cofactor II (HCII) inhibits thrombin rapidly in human plasma in the presence of heparin or dermatan sulfate. To determine the minimum structure of dermatan sulfate required to activate HCII, the glycosaminoglycan was partially degraded by seq
Publikováno v:
The Journal of Immunology. 138:285-292
Enhancement of binding of one monoclonal antibody to an antigen in the presence of a second monoclonal antibody (specific for an independent epitope on the same antigen) has been observed for several antigen-antibody systems involving primarily prote
Publikováno v:
The Journal of Immunology. 139:2702-2707
Using monoclonal anti-idiotopes with previously defined specificities for the variable (V) domain of HGAC 39, a monoclonal antibody against streptococcal group A carbohydrate (GAC), we have studied the effect of anti-idiotope on an anticarbohydrate i
Publikováno v:
Journal of Biological Chemistry. 258:6713-6716
We have tested the ability of various glycosaminoglycans to increase the rate of inhibition of thrombin by heparin cofactor II (HCII) and by antithrombin III (ATIII) isolated from human plasma. Heparin, dermatan sulfate, and heparan sulfate from bovi
Publikováno v:
Journal of immunology (Baltimore, Md. : 1950). 139(8)
Using monoclonal anti-idiotopes with previously defined specificities for the variable (V) domain of HGAC 39, a monoclonal antibody against streptococcal group A carbohydrate (GAC), we have studied the effect of anti-idiotope on an anticarbohydrate i
Publikováno v:
The Journal of biological chemistry. 261(19)
Heparin cofactor II (HCII) inhibits thrombin rapidly in human plasma in the presence of heparin or dermatan sulfate. To determine the minimum structure of dermatan sulfate required to activate HCII, the glycosaminoglycan was partially degraded by seq
Publikováno v:
The Journal of biological chemistry. 258(11)
We have tested the ability of various glycosaminoglycans to increase the rate of inhibition of thrombin by heparin cofactor II (HCII) and by antithrombin III (ATIII) isolated from human plasma. Heparin, dermatan sulfate, and heparan sulfate from bovi
Publikováno v:
Journal of immunology (Baltimore, Md. : 1950). 138(1)
Enhancement of binding of one monoclonal antibody to an antigen in the presence of a second monoclonal antibody (specific for an independent epitope on the same antigen) has been observed for several antigen-antibody systems involving primarily prote