Monoclonal antibody interferes with fibrin binding of t-PA.
Tissue-type plasminogen activator (t-PA) has a high affinity for fibrin, which is in contrast to urokinase-type plasminogen activator (u-PA). The relation between the structure and function of t-PA was investigated using monoclonal antibodies and plasmin digested t-PA fragments. The results obtained indicated that the three dimensional structure of kringle 2 is necessary for t-PA to develop its fibrin affinity. The monoclonal antibodies which interfered with the fibrin binding ability of native t-PA had two separate epitopes, one in kringle 2 and other in the N-terminal region of the light chain of t-PA.
Matsuo
O
O
Department of Physiology, Kinki University School of Medicine, Osakasayama, Japan.
Okada
K
K
Fukao
H
H
Tanaka
N
N
Ueshima
S
S
D000911:Antibodies, Monoclonal; D001665:Binding Sites; D000939:Epitopes; D005337:Fibrin / Q000276:immunology / Q000378:metabolism*; D005341:Fibrinolysin / Q000378:metabolism; D006801:Humans; D007120:Immunochemistry; D066298:In Vitro Techniques; D010446:Peptide Fragments / Q000276:immunology / Q000378:metabolism; D010958:Plasminogen / Q000378:metabolism; D010959:Tissue Plasminogen Activator / Q000276:immunology / Q000378:metabolism*
D000911:Antibodies, Monoclonal; D000939:Epitopes; D010446:Peptide Fragments; D005337:Fibrin; D010958:Plasminogen; D010959:Tissue Plasminogen Activator; D005341:Fibrinolysin