Zobrazeno 1 - 9
of 9
pro vyhledávání: '"C M Fitzsimmons"'
MAC188 S/S is a monoclonal antibody which can be used in vivo to measure the absolute number of functioning low-density lipoprotein (LDL) receptors in a rabbit. The antibody binds to the extra-cellular domain of the LDL receptor and binding is not bl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::97c421e43c597c017f12fb7d0275b16a
https://europepmc.org/articles/PMC1136343/
https://europepmc.org/articles/PMC1136343/
Publikováno v:
The Biochemical journal. 280
MAC188 is a rat anti-[low-density lipoprotein (LDL) receptor] monoclonal antibody (McAb) which binds to the cell surface receptor with high affinity at physiological temperatures, even in the presence of high concentrations of the natural ligand, LDL
Publikováno v:
Thrombosis and Haemostasis. 61:378-385
SummaryThe binding of fn to collagen (type I) fibres has been found to resemble that of vWf in the following respects: 1. Binding is rapid, specific, saturable, similar at 4 and 37°C, and reduced by increasing ionic strength.2. Binding is not inhibi
Publikováno v:
Thrombosis and Haemostasis. 59:186-192
SummaryFollowing fragmentation of the collagen molecule, we have examined the ability of the isolated fragments to bind vWf. In view of the importance of collagen tertiary and quaternary structure for binding, fragments were first renatured to restor
Publikováno v:
Thrombosis and haemostasis. 56(1)
In this study, the ability of peptides, obtained by fragmentation of the collagen type I molecule, to induce platelet aggregation has been examined. In order to satisfy requirements for tertiary and quaternary structure, peptides were first renatured
Collagen type III possesses a highly reactive platelet-aggregatory site at a locus which in type I is essentially inactive whilst the latter collagen possesses reactive sites absent in type III. It is proposed that platelet aggregation by collagen in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f32f1abbd2c8b2e13416c367dc5a6990
https://europepmc.org/articles/PMC1148567/
https://europepmc.org/articles/PMC1148567/
Publikováno v:
Thrombosis and haemostasis. 59(2)
Following fragmentation of the collagen molecule, we have examined the ability of the isolated fragments to bind vWf. In view of the importance of collagen tertiary and quaternary structure for binding, fragments were first renatured to restore tripl
Publikováno v:
Biochemical Society Transactions. 14:1086-1087
Publikováno v:
Biochemical Society Transactions. 14:1085-1086