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ATP binding to bovine serum albumin
Author(s) -
Bauer Michael,
Baumann Joachim,
Trommer Wolfgang E.
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)81211-4
Subject(s) - bovine serum albumin , moiety , chemistry , nucleotide , binding site , serum albumin , adenosine triphosphate , molar concentration , biochemistry , albumin , plasma protein binding , stereochemistry , stoichiometry , stearic acid , chromatography , organic chemistry , gene
Specific binding or ATP to bovine serum albumin (BSA) is demonstrated employing ATP derivatives spin‐labeled at either N 6 or C8 of adenine ring or at the ribose moiety. Based on a 1:1 stoichiometry binding constants are in the 50–100 μM 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.