Purification and characterization of a calmodulin-dependent myosin heavy chain kinase from intestinal brush border.

Szczegóły
Abstrakt

Tytuł:: Purification and characterization of a calmodulin-dependent myosin heavy chain kinase from intestinal brush border.
Autorzy:: Rieker JP; Department of Microbiology, Biochemistry, and Molecular Biology, School of Medicine, University of Pittsburgh, Pennsylvania 15261.
Swanljung-Collins H
Collins JH
Źródło:: The Journal of biological chemistry [J Biol Chem] 1987 Nov 05; Vol. 262 (31), pp. 15262-8.
Typ publikacji:: Journal Article; Research Support, U.S. Gov't, P.H.S.
Język:: English
Imprint Name(s):: Publication: 2021- : [New York, NY] : Elsevier Inc. on behalf of American Society for Biochemistry and Molecular Biology
Original Publication: Baltimore, MD : American Society for Biochemistry and Molecular Biology
MeSH Terms:: Calcium-Calmodulin-Dependent Protein Kinases*
Calmodulin/*pharmacology
Intestine, Small/*enzymology
Microvilli/*enzymology
Phosphotransferases/*isolation & purification
Animals ; Chickens ; Chromatography, Affinity ; Chromatography, Gel ; Chromatography, High Pressure Liquid ; Chromatography, Ion Exchange ; Kinetics ; Molecular Weight ; Phosphotransferases/metabolism ; Protozoan Proteins
Grant Information:: 5T32 HL07557 United States HL NHLBI NIH HHS; GM 32567 United States GM NIGMS NIH HHS; GM 35448 United States GM NIGMS NIH HHS
Substance Nomenclature:: 0 (Calmodulin)
0 (Protozoan Proteins)
EC 2.7.- (Phosphotransferases)
EC 2.7.11.17 (Calcium-Calmodulin-Dependent Protein Kinases)
EC 2.7.11.7 (myosin-heavy-chain kinase)
Entry Date(s):: Date Created: 19871105 Date Completed: 19871210 Latest Revision: 20210210
Update Code:: 20240104
PMID:: 2822719
: Czasopismo naukowe

A calcium- and calmodulin-dependent kinase that represents the majority of the myosin heavy chain kinase activity in chicken intestinal brush borders has been highly purified. The purification steps include gel filtration, high performance chromatography on anion and cation exchangers, and affinity chromatography on calmodulin-Sepharose. The purified kinase consists of a single major, apparently autophosphorylatable polypeptide of 50,000 daltons. The Stokes radius (68 A) and sedimentation coefficient (17.5 S) indicate that it has a molecular weight of approximately 490,000. The kinase catalyzed the incorporation of a maximum of 0.8 mol of phosphate/mol of heavy chain, and essentially no phosphate was incorporated into the light chains. This kinase is distinct from other myosin kinases, but has a number of properties in common with the type II calmodulin-dependent protein kinases.

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