The cleavage of β‐chain in bovine fibrinogen DH fragment (95 kDa) leads to a significant increase in its anticlotting activity

FEBS Letters

Litvinovich, S.V.¹  Lukinova, N.I.¹  Platonova, T.N.¹  Medved', L.V.¹ 

[1] Institute of Biochemistry, Academy of Sciences of the Ukrainian SSR, Kiev, USSR

关键词: Fragment DH;    Anticlotting activity;    Proteolysis;    Activation;    Sequence homology;   

DOI  :  10.1016/0014-5793(88)80385-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

It is shown that in the presence of Ca²⁺ plasmin converts bovine fibrinogen fragment D_H (95 kDa) into D_LA fragment by the cleavage of its β-chain Arg₃₇₂Thr₃₇₃ 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 Arg₃₇₂Thr₃₇₃ bond bears some resemblance to the general activation of proenzyme into enzyme.

【 授权许可】

Unknown