Structure of fragment E species from human cross-linked fibrin.

摘要: Abstract Fragments E1, E2, and E3 are plasmic derivatives of fibrin encompassing the NH2-terminal region molecule. The first two species, but not third, can bind to fragment DD, forming a (DD)E complex, therefore probably contain binding sites involved in polymerization fibrin. For localization these structure fragments was determined by establishing NH2- COOH-terminal boundaries molecules using published amino acid sequence fibrinogen. Fragment E1 encompasses Gly-alpha 17 Lys-alpha 78, Gly-beta 15 Lys-beta 122, Tyr-gamma 1 Lys-gamma 62, this representing intact E2 is an asymmetric molecule which lacking 53 one beta-chain remnant. This also lost 122 from COOH terminal beta chain as compared with E1. These cleavages did affect ability DD. heterogeneous, main species Val-alpha 20 54 Leu-beta 120, 53. Thus, loss function formation clot associated removal small all three polypeptide chains: alpha 17-19 (Gly-Pro-Arg), 15-53 remaining half molecule, 121 (Leu), gamma 54-58 (Thr-Ser-Glu-Val-Lys).