Title : Protein aggregation mediated by cysteine oxidation during the stacking phase of discontinuous buffer SDS-PAGE.

Pub. Date : 2001 Feb

PMID : 11233600






7 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 Recombinant human interferon-inducible protein-10 (IP-10), a 10-kDa C-X-C chemokine with four cysteines, aggregated during the stacking phase of SDS-PAGE and generated a band with an apparent molecular mass of 18 kDa. Cysteine C-X-C motif chemokine ligand 10 Homo sapiens
2 Recombinant human interferon-inducible protein-10 (IP-10), a 10-kDa C-X-C chemokine with four cysteines, aggregated during the stacking phase of SDS-PAGE and generated a band with an apparent molecular mass of 18 kDa. Cysteine C-X-C motif chemokine ligand 10 Homo sapiens
3 Recombinant human interferon-inducible protein-10 (IP-10), a 10-kDa C-X-C chemokine with four cysteines, aggregated during the stacking phase of SDS-PAGE and generated a band with an apparent molecular mass of 18 kDa. Sodium Dodecyl Sulfate C-X-C motif chemokine ligand 10 Homo sapiens
4 Recombinant human interferon-inducible protein-10 (IP-10), a 10-kDa C-X-C chemokine with four cysteines, aggregated during the stacking phase of SDS-PAGE and generated a band with an apparent molecular mass of 18 kDa. Sodium Dodecyl Sulfate C-X-C motif chemokine ligand 10 Homo sapiens
5 This aggregation depended on the presence of reduced sulfhydryl residues on IP-10, on the amount of loaded protein, and on the concentration of the ammonium persulfate used to polymerize the stacking gel. Sulfhydryl Compounds C-X-C motif chemokine ligand 10 Homo sapiens
6 The aggregation of IP-10 could be prevented by reduction of its sulfhydryls with dithiothreitol followed by irreversible blockade with iodoacetamide. Dithiothreitol C-X-C motif chemokine ligand 10 Homo sapiens
7 The aggregation of IP-10 could be prevented by reduction of its sulfhydryls with dithiothreitol followed by irreversible blockade with iodoacetamide. Iodoacetamide C-X-C motif chemokine ligand 10 Homo sapiens