Abstract
Phenylglyoxal (PGO) was used as a reagent for chemical modification of the ATP-binding site of Ca2+-transporting ATPase of rabbit skeletal muscle sarcoplasmic reticulum (SR-ATPase). When 1 mM PGO was reacted with SR-ATPase at 30°C at pH 8.5, PGO was bound to the ATPase molecule in two-to-one stoichiometry with concomitant loss of activity of the ATPase to form the phosphorylated intermediate (E-P). ATP and ADP prevented the binding of PGO and thereby protected the enzyme from inactivation. The SR membranes were labeled with [14C]PGO and then digested with pepsin to identify the attachment site of PGO. A 14C-labeled peptide (402lle-Arg*-Ser-Gly-Gln406) was purified to homogeneity by C18-reversed phase HPLC (Arg* denotes the binding site of [14C]PGO). These results indicate that Arg403 is located in the ATP binding site of the SR-ATPase. (Mol Cell Biochem 190: 169–177, 1999)
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Dedicated to Dr. Setsuro Ebashi who pioneered the field of Ca2+-mediated regulation of physiological processes.
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Yamamoto, H., Kawakita, M. (1999). Chemical modification of an arginine residue in the ATP-binding site of Ca2+-transporting ATPase of sarcoplasmic reticulum by phenylglyoxal. In: Imai, S., Ohtsuki, I., Endo, M. (eds) Muscle Physiology and Biochemistry. Molecular and Cellular Biochemistry, vol 31. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-5543-8_21
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