Dephosporylation with alkaline phosphatase of histone and fibrinogen phosphorylated with protein kinase C in vitro.

Abstract:

: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.

journal_name

Ups J Med Sci

authors

Ekman P

doi

10.3109/03009739109179262

subject

Has Abstract

pub_date

1991-01-01 00:00:00

pages

95-102

issue

2

eissn

0300-9734

issn

2000-1967

journal_volume

96

pub_type

杂志文章
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