Conformational changes in human fibrinogen after in vitro phosphorylation and their relation to fibrinogen behaviour

FEBS Letters

Björk, Ingemar²  Martin, Steven C.¹ 

[1] Department of Medical and Physiological Chemistry, Uppsala University, Box 575, S-751 23 Uppsala, Sweden;Department of Veterinary Medical Chemistry, Swedish University of Agricultural Sciences, Uppsala Biomedical Centre, Box 575, S-751 23 Uppsala, Sweden

关键词: Fibrinogen;    Protein phosphorylation;    Protein kinase;    Circular dichroism;    Fluorescence;   

DOI  :  10.1016/0014-5793(90)80458-U

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The far-ultraviolet circular dichroism spectra of fibrinogens phosphorylated by protein kinase C or casein kinase II indicated a conformational change corresponding to an increase in ordered secondary structure. The spectra of protein kinase A- or casein kinase I-phosphorylated fibrinogens did not differ substantially from the control. Fluorescence studies indicated changes in the tertiary structure around tryptophan residues for protein kinase A- or C-phosphorylated fibrinogens, but failed to show any such change for fibrinogen phosphorylated by either of the casein kinases. This latter result was also confirmed by circular dichroism measurements in the near-ultraviolet region. The apparent increase in ordered structure was proposed as an explanation for the slower rate of plasmin degradation seen in fibrinogens after phosphorylation by protein kinase C [6], and casein kinase II, especially as both spectral changes and plasmin degradation rate were unaffected by alkaline phosphatase.

【 授权许可】

Unknown