Proton NMR structural characterization of a recombinant kringle 2 domain from human tissue-type plasminogen activator

Biochemistry ◽  
1989 ◽  
Vol 28 (24) ◽  
pp. 9350-9360 ◽  
Author(s):  
In Ja L. Byeon ◽  
Robert F. Kelley ◽  
Miguel Llinas
Keyword(s):  
Plasminogen Activator ◽  
Structural Characterization ◽  
Human Tissue ◽  
Proton Nmr ◽  
Tissue Type ◽  
Tissue Type Plasminogen Activator ◽  
Type Plasminogen Activator ◽  
Kringle 2

Ligand Binding to the Tissue-Type Plasminogen Activator Kringle 2 Domain: Structural Characterization by 1H-NMR

Biochemistry ◽  
1995 ◽  
Vol 34 (9) ◽  
pp. 2739-2750 ◽  
Author(s):  
In-Ja L. Byeon ◽  
Robert F. Kelley ◽  
Michael G. Mulkerrin ◽  
Seong Soo A. An ◽  
Miguel Llinas
Keyword(s):  
Ligand Binding ◽  
Plasminogen Activator ◽  
1H Nmr ◽  
Structural Characterization ◽  
Tissue Type ◽  
Tissue Type Plasminogen Activator ◽  
Type Plasminogen Activator ◽  
Kringle 2

Characterization of Two Monoclonal Antibodies Against Human Tissue-Type Plasminogen Activator

1985 ◽  
Vol 53 (02) ◽  
pp. 170-175 ◽  
Author(s):  
Raymond R Schleef ◽  
Manjula Sinha ◽  
David J Loskutoff
Keyword(s):  
Monoclonal Antibodies ◽  
Plasminogen Activator ◽  
Human Tissue ◽  
Association Constant ◽  
Tissue Type ◽  
Tissue Type Plasminogen Activator ◽  
High Affinity ◽  
Standard Procedures ◽  
Type Plasminogen Activator

SummaryA series of hybridoma clones, each producing monoclonal antibodies to human tissue-type plasminogen activator (t-PA), were prepared from mice by standard procedures. Two of these clones were selected for further study. One HI72A1, produced antibodies that bound to t-PA and strongly inhibited its activity, whereas another, LI72D1, produced antibodies that bound to t-PA but did not affect its activity. The specificity of these antibodies was assessed in immunoabsorption experiments. Both immunoprecipitated 125I-labeled t-PA, and both were specific since only t-PA was recognized in conditioned media collected from Bowes melanoma cells cultured in the presence of 3H-leucine. Neither antibody recognized urokinase. t-PA was desorbed from antibody HI72A1-Sepharose columns with 0.5 M NaCl, consistent with its relatively low association constant (Ka = 9.37 × 107 M-1). In contrast, a strong chaotropic agent (i.e., 2 M KI) was required to elute t-PA from antibody LI72D1 columns (Ka = 2.08 × 109 M-1). This latter high affinity antibody was employed to develop an immunoradiometric assay for t-PA having a sensitivity of 0.5 ng/ml.

Characterization of a Panel of Monoclonal Antibodies Against Human Tissue-Type Plasminogen Activator

Hybridoma ◽  
1988 ◽  
Vol 7 (2) ◽  
pp. 177-184 ◽  
Author(s):  
THOMAS M. REILLY ◽  
SANDRA K. FLINT ◽  
BERNIE G. McHUGH ◽  
KATHLEEN M. WILSBACH-VOLCHECK ◽  
PIETER B.M.W.M. TIMMERMANS
Keyword(s):  
Monoclonal Antibodies ◽  
Plasminogen Activator ◽  
Human Tissue ◽  
Tissue Type ◽  
Tissue Type Plasminogen Activator ◽  
Type Plasminogen Activator

scholarly journals Characterization of the Binding of Human Tissue-type Plasminogen Activator to Platelets

1989 ◽  
Vol 264 (27) ◽  
pp. 15869-15874
Author(s):  
D E Vaughan ◽  
M E Mendelsohn ◽  
P J Declerck ◽  
E Van Houtte ◽  
D Collen ◽  
...  
Keyword(s):  
Plasminogen Activator ◽  
Human Tissue ◽  
Tissue Type ◽  
Tissue Type Plasminogen Activator ◽  
Type Plasminogen Activator
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