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The cleavage of β‐chain in bovine fibrinogen D H fragment (95 kDa) leads to a significant increase in its anticlotting activity
Author(s) -
Medved' L.V.,
Platonova T.N.,
Litvinovich S.V.,
Lukinova N.I.
Publication year - 1988
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(88)80385-5
Subject(s) - thermolabile , cleavage (geology) , chemistry , fragment (logic) , bond cleavage , covalent bond , plasmin , stereochemistry , fibrinogen , enzyme , biochemistry , biology , catalysis , organic chemistry , paleontology , fracture (geology) , computer science , programming language
It is shown that in the presence of Ca 2+ plasmin converts bovine fibrinogen fragment D H (95 kDa) into D LA fragment by the cleavage of its β‐chain Arg 372 Thr 373 bond. D LA fragment consists of two components (82 and 12 kDa) held together by non‐covalent bonds and has 3.5‐fold higher anticlotting activity than D H fragment. The D H to D LA 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 D H fragment by the cleavage of its Arg 372 Thr 373 bond bears some resemblance to the general activation of proenzyme into enzyme.