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Forschungsdatenbank PMU-SQQUID

Metavinculin and vinculin from mammalian smooth muscle: bulk isolation and characterization.
Gimona, M; Fürst, DO; Small, JV;
J Muscle Res Cell Motil. 1987; 8(4): 329-341.
Originalarbeiten (Zeitschrift)


Gimona Mario


Metavinculin, a vinculin related protein found only in muscle, has been prepared in bulk amounts from porcine stomach by a new procedure: the same procedure is applicable to the purification of vinculin from porcine stomach and avian gizzard. A comparison of the mammalian and avian proteins by peptide mapping showed them all to contain a common protease resistant 90 kDa core; however both avian and mammalian vinculins were notably more resistant to proteolysis down to this core than their respective metavinculins. Despite the close similarities in the peptide maps, in molecular weight and amino acid composition neither of the mammalian proteins exhibited the head and tail morphology formerly described for gizzard vinculin and metavinculin; both porcine proteins appeared globular under the electron microscope. From the gross variability in the ratios of metavinculin to vinculin among smooth muscles of different origin as well as from the common detergent-independent solubility properties of both proteins during isolation, it is concluded that vinculin and metavinculin perform duplicatory roles as peripheral membrane components. No definitive evidence for the interaction of either protein with actin filaments was obtained.

Useful keywords (using NLM MeSH Indexing)


Avian Proteins*

Calmodulin-Binding Proteins/analysis

Immunologic Techniques

Isoelectric Point

Microscopy, Electron

Molecular Weight

Muscle Proteins/isolation*


Muscle, Smooth/analysis*

Peptide Mapping

Protein Conformation