Fibrin aggregation. The effect of a fibrin specific monoclonal antibody on the aggregation process

Edgell, Tracey A.; Gaffnev, P.J.; Hockley, David J.; Webbon, P. M.; Walker, J L

doi:10.1016/0268-9499(94)90387-5

Cited by 1 publication

(2 citation statements)

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“…The Kd for baboon pads was nearly 100 greater than for human fibrin pads while the Kd for fibrin monolayers differed by a factor of 3-7000. These mabs have been reported to be directed to linear sequences on the Aa chain of fibrinogen near the carboxy terminus of this chain (13). While the loca tion of this epitope needs more rigorous proof than currently available it is tentatively suggested that this region may differ significantly in primary sequence between the human and baboon species.…”

Section: Discussionmentioning

confidence: 99%

“…This partial characterisation indicated, apart from fibrin specificity, that the mabs 12B3B10 and 12B3A11 both reacted with the a chain of fibrin while 5F3 reacted with the p chain. Subsequent data (S. Raut et al, unpublished work) had shown that IH10 and 5F3 react only with the E domain of fibrin while 12B3B10 and 12B3A11 have been subsequently shown to react with the carboxy region of the a chain (13). Horseradish peroxidase (HRP) conjugated rabbit anti-mouse (RAM) antibody was obtained from Dakopatts A/S (Glostrup, Denmark).…”

Section: Methodsmentioning

confidence: 99%

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Monoclonal Antibodies to Human Fibrin: Interaction with other Animal Fibrins

et al. 1996

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SummaryFour monoclonal antibodies have previously been raised in our laboratory for possible use in thrombus imaging and the targeting of thrombolytic agents. These antibodies were raised to various human fibrin-related immunogens and each antibody had been selected for its specificity towards fibrin and not fibrinogen. To study further these antibodies in animal circulation models both in vivo and in vitro, their selectivity towards human fibrin as opposed to other animal fibrins was examined. In this study dissociation constants for each antibody with each of six species fibrins (human, baboon, pig, dog, sheep, and rabbit) were estimated using both fibrin clots and monolayers. Some limited data were also obtained with Sepharose-fibrin. Of the antibodies two (denoted 12B3B10 and 12B3A11) are seen to bind almost exclusively to human fibrin with dissociation constants of about 8 × 10−10 M using fibrin clots and monolayers. These same two mabs bound to baboon fibrin with a dissociation constant of 2 × 10−9 M, while neither displayed significant levels of binding to the fibrins from dog, pig, sheep and rabbit. The other two antibodies investigated (1H10 and 5F3) were found to bind well to fibrins of human, baboon, pig and dog, with dissociation constants in the range of 1.4-4.2 × 10−9 M. However neither 1H10 nor 5F3 displayed significant recognition of sheep and rabbit fibrins. Both 1H10 and 5F3 were also found by means of competitive ELISA’s to retain their selectivity to baboon, dog and pig fibrins in the presence of their respective fibrinogens.

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Section: Discussionmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%