Connexon integrity is maintained by non-covalent bonds: Intramolecular disulfide bonds link the extracellular domains in rat connexin-43

Rat heart connexin-43 (RC×43) has been isolated using a modified procedure that is rapid and can be used with fresh or frozen hearts. When RC×43 is isolated in the presence of the alkylating reagent iodoacetamide, no intermolecular disulfide bonds are found. However, the alkylated RC×43 does have at...

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Veröffentlicht in:	Biochemical and biophysical research communications 1991-08, Vol.178 (3), p.1312-1318
Hauptverfasser:	John, Scott A., Revel, Jean-Paul
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Animals Antibodies Biological and medical sciences Cell interactions, adhesion Connexins Disulfides - analysis Fundamental and applied biological sciences. Psychology Humans Immunoblotting Iodoacetamide - pharmacology Membrane Proteins - chemistry Membrane Proteins - genetics Membrane Proteins - isolation & purification Molecular and cellular biology Molecular Sequence Data Myocardium - metabolism Peptide Fragments - isolation & purification Peptides - chemical synthesis Protein Conformation Rats Rats, Inbred Strains Sequence Homology, Nucleic Acid
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Zusammenfassung:	Rat heart connexin-43 (RC×43) has been isolated using a modified procedure that is rapid and can be used with fresh or frozen hearts. When RC×43 is isolated in the presence of the alkylating reagent iodoacetamide, no intermolecular disulfide bonds are found. However, the alkylated RC×43 does have at least one intramolecular disulfide bond. By using site directed antibodies and proteolytic cleavage the location of the intramolecular disulfide bonding is shown between the two extracellular loops of RC×43.
ISSN:	0006-291X 1090-2104
DOI:	10.1016/0006-291X(91)91037-D