Linked Life Data

8586621

Source:http://linkedlifedata.com/resource/pubmed/id/8586621

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1996-3-25
pubmed:abstractText
The activity of calmodulin-dependent protein kinase IV (CaM-kinase IV) was progressively decreased by incubation at 30 degrees C with calmodulin in the presence of Ca2+, becoming one-half to one-fifth of the original activity within several minutes. The amount of calmodulin necessary to produce the maximal inactivation was approximately 1 mol for 1 mol of the enzyme. The inactivation of CaM-kinase IV by Ca2+/calmodulin was prevented by ATP in the presence of Mg2+, but such protection was not observed with either of the two alone or with a peptide substrate such as syntide-2. The activity of the calmodulin-inactivated enzyme was increased by incubation at 30 degrees C with Mg2+ in the presence of EGTA, being completely restored to the original level within several minutes, indicating that the Ca2+/calmodulin-induced inactivation of the enzyme was not due to irreversible denaturation of the enzyme. Both the inactivation of CaM-kinase IV by Ca2+/calmodulin and the restoration of its activity by Mg2+/EGTA were time- and temperature-dependent reactions. Kinetic analysis revealed that the alterations of the enzyme activity were due mainly to changes in Vmax of the enzyme.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0021-924X
pubmed:author
pubmed:issnType
Print
pubmed:volume
117
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1070-5
pubmed:dateRevised
2007-12-19
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
Inactivation of Ca2+/calmodulin-dependent protein kinase IV by Ca2+/calmodulin and restoration of the activity by Mg2+/EGTA.
pubmed:affiliation
Department of Biochemistry, Asahikawa Medical College, Hokkaido.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't