Isolation and localization of filamin in heart muscle

High‐molecular‐mass protein was isolated from chicken heart muscle. The apparent molecular mass of a single polypeptide chain is similar to that of chicken gizzard filamin: 250–270 kDa. The protein interacts with antibodies against chicken gizzard filamin and induces F‐actin gelation in a concentrat...

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Veröffentlicht in:	European journal of biochemistry 1986-05, Vol.156 (3), p.619-623
Hauptverfasser:	KOTELIANSKY, Victor E., GLUKHOVA, Marina A., GNEUSHEV, Gennady N., SAMUEL, Jane‐Lyse, RAPPAPORT, Lydie
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Applied sciences Chickens Chromatography, DEAE-Cellulose Contractile Proteins - isolation & purification Electrophoresis, Polyacrylamide Gel Enzyme-Linked Immunosorbent Assay Exact sciences and technology filamin Filamins Fluorescent Antibody Technique Gizzard, Avian heart Microfilament Proteins - isolation & purification Microscopy, Phase-Contrast muscles Myocardium - analysis Myocardium - ultrastructure Myofibrils - analysis Myofibrils - ultrastructure Other techniques and industries
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Beschreibung
Zusammenfassung:	High‐molecular‐mass protein was isolated from chicken heart muscle. The apparent molecular mass of a single polypeptide chain is similar to that of chicken gizzard filamin: 250–270 kDa. The protein interacts with antibodies against chicken gizzard filamin and induces F‐actin gelation in a concentration‐dependent manner. Immunofluorescent staining of cardiomyocytes and chicken heart sections with antifilamin antibody demonstrates two types of filamin localization: (a) filamin was located on the sarcomete border in the periphery of the Z‐disk; (b) filamin was found in intercalated disks between cardiomyocytes.
ISSN:	0014-2956 1432-1033
DOI:	10.1111/j.1432-1033.1986.tb09622.x