Rat pancreas actin: Purification and characterization

Isolation of rat pancreas actin was performed with three different technics: polymerization-depolymerization method, affinity chromatography on DNase I-Sepharose 4B or ion exchange chromatography on DEAE-cellulose. Inhibition of DNase I activity, localization by SDS polyacrylamide slab gel electroph...

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Bibliographic Details
Published inBiochemical and biophysical research communications Vol. 113; no. 1; pp. 163 - 170
Main Authors Gendry, P., Launay, J.F., Vanier, M.T.
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 31.05.1983
Subjects
actin
Actins - isolation & purification
Animals
Chromatography, Affinity
Chromatography, DEAE-Cellulose
Deoxyribonuclease I
Electrophoresis, Polyacrylamide Gel
Endodeoxyribonucleases - metabolism
Microscopy, Electron
pancreas
Pancreas - analysis
Polymers
Rats
DTE
DNase I
ATP
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Summary:Isolation of rat pancreas actin was performed with three different technics: polymerization-depolymerization method, affinity chromatography on DNase I-Sepharose 4B or ion exchange chromatography on DEAE-cellulose. Inhibition of DNase I activity, localization by SDS polyacrylamide slab gel electrophoresis and presence of microfilaments allowed its identification. Affinity process led us to obtain actin which kept inhibitory activity (30,000 U per mg) on DNase I when using vacuum dialysis. Actin eluted from DEAE-cellulose associated reversibly in 50–70 Å microfilaments in the presence of phalloidin, was pure at 95% and had a satisfactory inhibitor activity (77,000 U per mg).
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:0006-291X
1090-2104
DOI:10.1016/0006-291X(83)90446-1