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JBC, Vol. 250, Issue 1, 218-225, Jan, 1975
J. D. Corbin, S. L. Keely and C. R. Park
In crude extracts of adipose tissue the protein kinase dissociates slowly
at 30 degrees into regulatory and catalytic subunits in the presence of 700
mug per ml of histone or 0.5 M NaCl. If the kinase is first dissociated by
adding 10 muM adenosine 3':5'-monophosphate (cAMP), reassociation occurs
instantaneously after removal of the cAMP by Sephadex G-25 chromatography.
In contrast, in crude xtracts of heart, the protein kinase dissociates
rapidly in the presence of 700 mug per ml of histone or 0.5 M NaCl and
reassociates slowly after removal of cAMP. These differences are accounted
for by the existence of two types of protein kinases in these tissues,
referred to as types I and II. DEAE-cellulose chromatography of extracts of
adipose tissue produces only one peak of cAMP-dependent protein kinase
activity (type II) which elutes between 0.15 and 0.25 M NaCl. Similar
chromatography of heart extracts resolves enzyme activity into two peaks; a
type I enzyme which elutes between 0.05 and 0.1 M and predominates (greater
than 75% of total activity), and a type II enzyme which elutes between 0.15
and 0.25 M NaCl. The dissociation properties of the types I and II enzymes
from heart and adipose tissue are retained after partial purification by
DEAE-cellulose and Sepharose 6B chromatography. Rechromatography of the
separated peaks of the cardiac enzymes does not change the elution pattern.
Sucrose density gradient centrifugation and gel filtration studies indicate
that the molecular weights of these enzymes are very similar. The type II
enzyme isolated by DEAE-cellulose chromatography of heart extracts
resembles the adipose tissue enzyme, i.e. it undergoes slow dissociation at
30 degrees in the presence of histone or 0.5 M NaCl. The adipose tissue
kinase and the heart type II kinase are not identical, however, since they
do not elute at exactly the same point on DEAE-cellulose columns. A survey
of several tissues indicates the presence of type I and II protein kinases
similar to the enzymes in adipose tissue and heart as determined by
DEAE-cellulose chromatography of crude extracts and by dissociation of the
enzymes with histone. The presence of MgATP prevents dissociation of type I
enzyme from heart by 0.5 M NaCl or histone. The profile of the enzyme on
DEAE-cellulose, however, is not changed...
The distribution and dissociation of cyclic adenosine 3':5'-monophosphate-dependent protein kinases in adipose, cardiac, and other tissues
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