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D A Skaleris

Publications and source records attributed to D A Skaleris.

2 recordsLinked to original sources

Interaction of DnaK with ATP: binding, hydrolysis and Ca+2-stimulated autophosphorylation.

The autophosphorylation of DnaK from Escherichia coli using ATP as phosphate donor is markedly stimulated by Ca+2 and to a lesser degree by Mn+2. Mg+2 and other divalent ions are without effect in this reaction. Lanthanum, an agonist/antagonist of Ca+2, is also effective in stimulating the autophosphorylation. In contrast, Mg+2 but not Ca+2, markedly stimulates the hydrolysis of ATP catalyzed by DnaK. Also at 0 degrees, ATP forms a stable complex with DnaK without hydrolysis that is independent of cations. About 15% of the DnaK in E. coli is associated with membrane vesicles where it also can be phosphorylated in the presence of Ca+2.

Adenosine Triphosphate↗

Human interleukin-2 anti-idiotypes.

We describe the generation of a monoclonal anti-idiotypic (anti-id) antibody directed against affinity purified rabbit antibodies (id) to recombinant human IL-2. This monoclonal antibody, 6A12, has the ability to inhibit the neutralization of IL-2 activity by the id, suggesting that it may bind at or near the IL-2 neutralizing site on the id. 6A12 exhibits IL-2 agonist activity on PHA-activated human T cells. The purified IgG of 6A12 is also shown to bind to a purified soluble recombinant p55 subunit of the IL-2 receptor. Furthermore, purified 6A12 shows inhibition of IL-2 activity in an IL-2 dependent mouse T cell line (CTLL) and this inhibition can be reversed by excess IL-2. These results suggest that although 6A12 may not be an exact 'internal image' of the receptor binding site of IL-2, it may bind to at least the P55 subunit of the ligand binding site on the high affinity IL-2 receptor complex.

Animals↗