Oligosaccharide epitopes and antibody binding sites of Fab and single chain Fv molecules

1996 ◽  
Vol 2 (4) ◽  
pp. 262
1991 ◽  
Vol 10 (6) ◽  
pp. 669-683 ◽  
Author(s):  
John E. McCartney ◽  
Lynne Lederman ◽  
Eric A. Drier ◽  
Nancy A. Cabral-Denison ◽  
Gay-May Wu ◽  
...  

FEBS Letters ◽  
1998 ◽  
Vol 425 (3) ◽  
pp. 479-484 ◽  
Author(s):  
Lynne J. Lawrence ◽  
Alexander A. Kortt ◽  
Peter Iliades ◽  
Peter A. Tulloch ◽  
Peter J. Hudson

1989 ◽  
Vol 62 (02) ◽  
pp. 699-703 ◽  
Author(s):  
Rob J Aerts ◽  
Karin Gillis ◽  
Hans Pannekoek

SummaryIt has recently been shown that the fibrinolytic components plasminogen and tissue-type plasminogen activator (t-PA) both bind to cultured human umbilical vein endothelial cells (HUVEC). After cleavage of t-PA by plasmin, “single-chain” t-PA (sct-PA) is converted into “two-chain” t-PA (tct-PA), which differs from the former in a number of respects. We compared binding of sct-PA and tct-PA to the surface of HUVEC. Removal of t-PA bound to HUVEC by a mild treatment with acid and a subsequent quantification of eluted t-PA both by activity- and immunoradiometric assays revealed that, at concentrations between 10 and 500 nM, HUVEC bind about 3-4 times more sct-PA than tct-PA. At these concentrations, both sct-PA and tct-PA remain active when bound to HUVEC. Mutual competition experiments showed that sct-PA and tct-PA can virtually fully inhibit binding of each other to HUVEC, but that an about twofold higher concentration of tct-PA is required to prevent halfmaximal binding of sct-PA than visa versa. These results demonstrate that sct-PA and tct-PA bind with different affinities to the same binding sites on HUVEC.


Biochemistry ◽  
1999 ◽  
Vol 38 (2) ◽  
pp. 532-539 ◽  
Author(s):  
Hiroyuki Kobayashi ◽  
Hiroshi Morioka ◽  
Kunihiro Tobisawa ◽  
Takuya Torizawa ◽  
Koichi Kato ◽  
...  

1993 ◽  
Vol 2 (2) ◽  
pp. 175-182 ◽  
Author(s):  
Christian Schwab ◽  
Andrea Twardek ◽  
Hans Rudolf Bosshard ◽  
Terence P. Lo ◽  
Gary D. Brayer

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