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ATP binding to bovine serum albumin
M Bauer1, J Baumann, W E Trommer
1Fachbereich Chemie, Universität Kaiserslautern, Germany.
FEBS Letters
|November 30, 1992
Abstract:
Specific binding of ATP to bovine serum albumin (BSA) is demonstrated employing ATP derivatives spin-labeled at either N6 or C8 of adenine ring or at the ribose moiety. Based on a 1:1 stoichiometry binding constants are in the 50-100 microM range. Binding is largely competitive with ATP or stearic acid. A small fraction of the labeled nucleotides could not be liberated by these ligands. Binding of AMP is in the millimolar range, only.