Fibrin fragment beta 15-118. Inhibitory and complex-forming properties
Lugovskoĭ, E.V.; Chudnovets, V.S.; Makogonenko, E.M.; Derzskaia, S.G.; Gogolinskaia, G.K.; Mikhalovskaia, L.I.; Komissarenko, S.V.
Ukrainskii Biokhimicheskii Zhurnal 67(4): 57-64
1995
ISSN/ISBN: 0201-8470 PMID: 8553474 Document Number: 445340
Peptide beta 15-118 isolated from desAABB-NDSK preserves fibrin polymerization active site "B", inhibits polymerization process at 12 degrees C, eliminates the inhibitory properties of plasmin D-D-fragment but does not influence inhibitory properties of a D-monomer fragment. Complex formation between peptide beta 15-118 and both D- and D-D fragments was electrophoretically demonstrated. Peptide beta 15-118 forms more stable complex with the D-D fragment which does not dissociate in the medium of polymerizing fibrin as the complex of the peptide with monomer D fragment does. Gel filtration data confirm dimerization of D-monomer fragments after their complexing with beta 15-118. This phenomenon suggests that mutual affinity of D-domains in fibrin increases after loci interactions of the "B"-"b" type.