scholarly journals Variants of human tissue-type plasminogen activator. Fibrin binding, fibrinolytic, and fibrinogenolytic characterization of genetic variants lacking the fibronectin finger-like and/or the epidermal growth factor domains.

1988 ◽  
Vol 263 (2) ◽  
pp. 1023-1029
Author(s):  
G R Larsen ◽  
K Henson ◽  
Y Blue
Keyword(s):  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Plasminogen Activator ◽  
Genetic Variants ◽  
Human Tissue ◽  
Tissue Type ◽  
Tissue Type Plasminogen Activator ◽  
Type Plasminogen Activator ◽  
Epidermal Growth

scholarly journals Tyrosine 67 in the epidermal growth factor-like domain of tissue-type plasminogen activator is important for clearance by a specific hepatic receptor.

1992 ◽  
Vol 267 (14) ◽  
pp. 9668-9677 ◽  
Author(s):  
R Bassel-Duby ◽  
N.Y. Jiang ◽  
T Bittick ◽  
E Madison ◽  
D McGookey ◽  
...  
Keyword(s):  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Plasminogen Activator ◽  
Tissue Type ◽  
Tissue Type Plasminogen Activator ◽  
Type Plasminogen Activator ◽  
Epidermal Growth

Monoclonal antibodies directed against human tissue-type plasminogen activator: a characterization of their species specificity, affinity and heavy-chain binding

1987 ◽  
Vol 46 (1) ◽  
pp. 141-152 ◽  
Author(s):  
J.F. Cajot ◽  
E. Bachmann ◽  
E. Cousin ◽  
E.K.O. Kruithof ◽  
W.D. Schleuning ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Plasminogen Activator ◽  
Heavy Chain ◽  
Human Tissue ◽  
Species Specificity ◽  
Tissue Type ◽  
Tissue Type Plasminogen Activator ◽  
Type Plasminogen Activator

Deglycosylation Increases the Fibrinolytic Activity of a Deletion Mutant of Tissue-Type Plasminogen Activator

1990 ◽  
Vol 63 (03) ◽  
pp. 464-471 ◽  
Author(s):  
James Wilhelm ◽  
Narender K Kalyan ◽  
Shaw Guang Lee ◽  
Wah-Tung Hum ◽  
Ruth Rappaport ◽  
...  
Keyword(s):  
Sialic Acid ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Fibrinolytic Activity ◽  
Deletion Mutant ◽  
Tissue Type ◽  
Side Chains ◽  
Tissue Type Plasminogen Activator ◽  
Type Plasminogen Activator ◽  
Epidermal Growth

SummaryΔ2−89 t-PA is a deletion mutant lacking the finger (F) and epidermal growth factor (EGF) domains; thus, the fibrin interaction of this molecule must be mediated solely by the kringle region. In the present study, the influence of the oligosaccharide side-chains on the activity of Δ2−89 t-PA has been investigated. Δ2−89 t-PA was secreted in two forms, designated I and II, which presumably differ by the lack of one asparagine-linked oligosaccharide in the kiiugle 2 domain of form TT, Forms I and II of Δ2−89 t-PA weie puiified; form II displayed higher fibrinolytic activity than form I. When foini I was partially deglycosylated or treated to remove sialic acid, fibrinolytic activity was increased. Production of Δ2−89 in the presence of timicamycin led to secielion of a glyean-free activator with higher activity. These findings suggest that certain oligusacchaiide side chains, particularly (hose containing sialic acid, can interfere with the interaction between the kringle region of t-PA and fibrin.

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.

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

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
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