Literature DB >> 2765564

Phosphorylation by cell surface protein kinase of bovine and human fibrinogen and fibrin.

J Sonka1, D Kübler, V Kinzel.   

Abstract

Human and bovine fibrinogen as well as fibrin are shown to be phosphorylated by Co631 (monolayer, hamster) and RPL12 (suspension, chicken) cells by their surface protein kinase of the casein kinase II type. The phosphate label is introduced into the alpha-peptide. The kinase system phosphorylates serine residues and utilizes GTP equally well as ATP. The participation of intact cell surfaces indicates the possibility of phosphorylation of extracellular fibrinogen independently of the site of its biosynthesis.

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Year:  1989        PMID: 2765564     DOI: 10.1016/0167-4838(89)90197-0

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  2 in total

Review 1.  Ecto-protein kinase CK2, the neglected form of CK2.

Authors:  Mathias Montenarh; Claudia Götz
Journal:  Biomed Rep       Date:  2018-02-21

2.  Stanniocalcin 1 and 2 are secreted as phosphoproteins from human fibrosarcoma cells.

Authors:  D A Jellinek; A C Chang; M R Larsen; X Wang; P J Robinson; R R Reddel
Journal:  Biochem J       Date:  2000-09-01       Impact factor: 3.857

  2 in total

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