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Last Updated: 3 years ago

Possible Interaction: Adenosine Triphosphate and Caseins

Research Papers that Mention the Interaction

ATP increased casein lysis by serine proteases, metalloprotease, and pepsin by 20-60% at concentration of 10(-3) M and by 30-260% at 10(-2) M concentration.
Bioorganicheskaia khimiia  •  2008  |  View Paper
The effects of basic compounds which affected dramatically the phosphorylation of dephosphorylated casein in presence of various ATP concentrations were reported.
The International journal of biochemistry  •  1994  |  View Paper
After complex formation, hydrolysis of Ub-protein conjugates and also the non-ubiquitinated substrate, casein , was stimulated severalfold by ATP , but non-metabolizable ATP analogs had little or no effect.
The Journal of biological chemistry  •  1990  |  View Paper
However, only ATP stimulated casein breakdown and only in the presence of Mg2+.
Proceedings of the National Academy of Sciences of the United States of America  •  1989  |  View Paper
When ubiquitin was removed by ion exchange chromatography, ATP still stimulated breakdown of casein and carbamylated casein twofold.
The Journal of cell biology  •  1983  |  View Paper
Addition of double-stranded or single-stranded DNA to the protease in the presence of ATP was found to stimulate the hydrolysis of casein or globin 2- to 7-fold, depending on the DNA concentration.
Proceedings of the National Academy of Sciences of the United States of America  •  1982  |  View Paper
Furthermore, ATP hydrolysis is stimulated two- to threefold by polypeptides that are substrates for the protease ( casein , glucagon) but not by nonhydrolyzed polypeptides (insulin, RNase).
Proceedings of the National Academy of Sciences of the United States of America  •  1982  |  View Paper