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Dephosphorylation with alkaline phosphatase of histone and fibrinogen phosphorylated with protein kinase C in vitro.
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical and Physiological Chemistry. (ek pia)
1991 (English)In: Upsala Journal of Medical Sciences, ISSN 0300-9734, E-ISSN 2000-1967, Vol. 96, no 2, 95-102 p.Article in journal (Refereed) Published
Abstract [en]

Alkaline phosphatase from calf intestinal mucosa dephosphorylated histone H1 and fibrinogen that had been phosphorylated with protein kinase C. The reaction velocity was dependent on the ionic strength of the buffer; decreasing with increasing concentration. The pH optimum was around 7, which is lower than pH-optima described for other kinds of substrates. (32P) phosphorylated fibrinogen was dephosphorylated about 20 times faster than (32P)phosphohistone on a weight basis and the reaction continued linearily with time for the longest time tested (3 hs) even at 37 degrees C. As alkaline phosphatase is present in the blood the possible physiological significance of the dephosphorylation of phosphofibrinogen is discussed.

Place, publisher, year, edition, pages
Scandinavian university press , 1991. Vol. 96, no 2, 95-102 p.
National Category
Biochemistry and Molecular Biology
URN: urn:nbn:se:uu:diva-172754PubMedID: 1776220OAI: oai:DiVA.org:uu-172754DiVA: diva2:515552
Available from: 2012-04-13 Created: 2012-04-13 Last updated: 2012-04-16Bibliographically approved

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