Identification of a complex between alpha-actinin and the intermediate filament subunit skeletin in bovine heart Purkinje fibres.

Abstract:

:A three-dimensional cytoskeleton, morphologically composed of intermediate filaments, desmosomes, and Z-disks, remains in bovine heart Purkinje fibres after extraction with Triton X-100 and low and high ionic strength solutions. Biochemically this cytoskeleton mainly consists of skeletin (Mr approximately 55 000) and of alpha-actinin (Mr approximately 95 000). Minor high molecular weight components are also present. By gel electrophoresis-derived enzyme-linked immunosorbent assay (GEDELISA) we show here that a 150 000-dalton component is a complex of alpha-actinin and skeletin. Furthermore, this 150 000-dalton component has now been purified and can be converted into 95 000- and 55 000-dalton subunits by reduction with a high concentration of beta-mercaptoethanol and heating. We also show that solubilized pure skeletin and pure alpha-ctinin from Purkinje fibres, after mixing, partly form a stable complex with a molecular weight of about 150 000 daltons.

journal_name

Eur J Cell Biol

authors

Kjörell U,Thornell LE

subject

Has Abstract

pub_date

1982-08-01 00:00:00

pages

139-44

issue

1

eissn

0171-9335

issn

1618-1298

journal_volume

28

pub_type

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