Reductive cleavage of the disulfide bonds of the collagen IV noncollagenous domain in aqueous sodium dodecyl sulfate: absence of intermolecular nondisulfide cross-links.

Reddy GK, Hudson BG, Bailey AJ, Noelken ME
Biochem Biophys Res Commun. 1993 190 (1): 277-82

PMID: 8422253 · DOI:10.1006/bbrc.1993.1042

The subunits of the collagen IV hexameric, noncollagenous NC1 domain obtained from bovine aorta, glomerular basement membrane, alveolar basement membrane and placental basement membrane are predominantly dimers. A large fraction of the dimers had been thought to be linked by nondisulfide bonds because they were resistant to cleavage by 5% (v/v) 2-mercaptoethanol, 2% (w/v) SDS, at 100 degrees C. However, if an unusually high concentration of 2-mercaptoethanol, e.g., 40% (v/v), is used, complete conversion of dimers into monomers is achieved, indicating the lack of intersubunit nondisulfide cross-links. Electrophoresis patterns indicate that some of the intermolecular disulfide bonds of the dimers are more resistant to reduction in aqueous SDS than are some of the intramolecular disulfide bonds.

MeSH Terms (23)

Alkylation Animals Aorta Basement Membrane Cattle Chromatography, High Pressure Liquid Collagen Cross-Linking Reagents Disulfides Dithiothreitol Electrophoresis, Polyacrylamide Gel Female Humans Hydrolysis Kidney Glomerulus Lysine Macromolecular Substances Mercaptoethanol Muscle, Smooth, Vascular Oxidation-Reduction Placenta Pregnancy Sodium Dodecyl Sulfate

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