The cleavage of beta-chain in bovine fibrinogen DH fragment (95 kDa) leads to a significant increase in its anticlotting activity.
It is shown that in the presence of Ca2+ plasmin converts bovine fibrinogen fragment DH (95 kDa) into DLA fragment by the cleavage of its beta-chain Arg372-Thr373 bond. DLA fragment consists of two components (82 and 12 kDa) held together by non-covalent bonds and has 3.5-fold higher anticlotting activity than DH fragment. The DH to DLA fragment conversion leads to the destabilization of thermolabile domains of the latter without the loss of their compact structure. The results obtained show that the activation of DH fragment by the cleavage of its Arg372-Thr373 bond bears some resemblance to the general activation of proenzyme into enzyme.
Medved
L V
LV
Institute of Biochemistry, Academy of Sciences of the Ukrainian SSR, Kiev, USSR.
Platonova
T N
TN
Litvinovich
S V
SV
Lukinova
N I
NI
D000595:Amino Acid Sequence; D000818:Animals; D001777:Blood Coagulation / Q000187:drug effects*; D002118:Calcium / Q000494:pharmacology*; D002417:Cattle; D004591:Electrophoresis, Polyacrylamide Gel; D005338:Fibrin Fibrinogen Degradation Products / Q000378:metabolism* / Q000494:pharmacology; D005341:Fibrinolysin / Q000378:metabolism*; D006801:Humans; D006868:Hydrolysis; D008969:Molecular Sequence Data; D008970:Molecular Weight; D012689:Sequence Homology, Nucleic Acid; D013329:Structure-Activity Relationship; D013816:Thermodynamics
D005338:Fibrin Fibrinogen Degradation Products; C015214:fibrinogen D fragment; D005341:Fibrinolysin; D002118:Calcium