Characterization of thrombospondin as a substrate for factor XIII transglutaminase.

@article{Lynch1987CharacterizationOT,
  title={Characterization of thrombospondin as a substrate for factor XIII transglutaminase.},
  author={G W Lynch and Henry S. Slayter and Bonnie E. Miller and J Mcdonagh},
  journal={The Journal of biological chemistry},
  year={1987},
  volume={262 4},
  pages={1772-8}
}
Thrombin activation of platelets induces the release of a high molecular weight glycoprotein, thrombospondin. On treatment with factor XIII transglutaminase and [3H]putrescine, thrombospondin undergoes specific incorporation of this labeled amine, with 2-3 mol of putrescine being incorporated per mol of thrombospondin. Analysis of plasmin digests of [3H]putrescine-thrombospondin showed that the Mr 53,000-core peptide contains the glutamine site for amine incorporation. In the absence of amine… CONTINUE READING

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Haemostasis: Biochemistry, Physiology and Pathology (Ogsten, D., and Bennet

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