[Fibrin fragment beta 15-118. Inhibitory and complex-forming properties].
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.
Lugovskoĭ
E V
EV
Chudnovets
V S
VS
Makogonenko
E M
EM
Derzskaia
S G
SG
Gogolinskaia
G K
GK
Mikhalovskaia
L I
LI
Komissarenko
S V
SV
D000933:Antifibrinolytic Agents / Q000737:chemistry*; D001704:Biopolymers; D001782:Blood Donors; D002850:Chromatography, Gel; D005337:Fibrin / Q000737:chemistry*; D005338:Fibrin Fibrinogen Degradation Products / Q000737:chemistry* / Q000494:pharmacology*; D006801:Humans; D010446:Peptide Fragments / Q000737:chemistry* / Q000494:pharmacology*; D011485:Protein Binding
D000933:Antifibrinolytic Agents; D001704:Biopolymers; D005338:Fibrin Fibrinogen Degradation Products; D010446:Peptide Fragments; C036309:fibrin fragment D; C097636:fibrin fragment beta (15-118); D005337:Fibrin
Fibrinovyĭ fragment beta 15-118. Ingibitornye i kompleksoobrazuiushchie svoĭstva.