Pub. Date : 2007 Feb 23
PMID : 17189254
7 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
1 | SDS-PAGE analysis showed that plasmin cleaved the heavy chain of factor VIII into two terminal products, A1(37-336) and A2 subunits, by limited proteolysis at Lys(36), Arg(336), Arg(372), and Arg(740). | Arginine | plasminogen | Homo sapiens |
2 | SDS-PAGE analysis showed that plasmin cleaved the heavy chain of factor VIII into two terminal products, A1(37-336) and A2 subunits, by limited proteolysis at Lys(36), Arg(336), Arg(372), and Arg(740). | Arginine | plasminogen | Homo sapiens |
3 | SDS-PAGE analysis showed that plasmin cleaved the heavy chain of factor VIII into two terminal products, A1(37-336) and A2 subunits, by limited proteolysis at Lys(36), Arg(336), Arg(372), and Arg(740). | Arginine | plasminogen | Homo sapiens |
4 | Plasmin-catalyzed cleavage at Arg(336) proceeded faster than that at Arg(372), in contrast to proteolysis by factor Xa. | Arginine | plasminogen | Homo sapiens |
5 | Plasmin-catalyzed cleavage at Arg(336) proceeded faster than that at Arg(372), in contrast to proteolysis by factor Xa. | Arginine | plasminogen | Homo sapiens |
6 | These results strongly indicated that cleavage at Arg(336) was a central mechanism of plasmin-catalyzed factor VIII inactivation. | Arginine | plasminogen | Homo sapiens |
7 | Furthermore, the cleavages at Arg(336) and Lys(36) appeared to be selectively regulated by the A2 and A3-C1-C2 domains, respectively, interacting with plasmin. | Arginine | plasminogen | Homo sapiens |