Summary
This paper summarizes our recent studies on pig gastric (H+ + K+)-ATPase. The amino acid sequence (from cDNA) of the pig enzyme was closely homologous to that of the rat enzyme. Functionally important amino acid residues for catalysis and ion translocation are pointed out. Chemical modification with pyridoxal 5′-phosphate suggested that Lys-497 may be located in the catalytic site or in its vicinity. DCCD inhibited the enzyme, possibly by cross-linking amino acid residues in the hydrophobic region of the enzyme.
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Maeda, M., Tamura, S., Futai, M. (1990). Structure and Chemical Modification of Pig Gastric (H++K+)-ATPase. In: Kim, C.H., Ozawa, T. (eds) Bioenergetics. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-5835-0_20
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DOI: https://doi.org/10.1007/978-1-4684-5835-0_20
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