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Partial Purification and Properties of the Inhibitors of Na,K‐ATPase and Ouabain‐Binding in Bovine Central Nervous System
Author(s) -
Akagawa Kimio,
Hara Naoyuki,
Tsukada Yasuzo
Publication year - 1984
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1984.tb02749.x
Subject(s) - amberlite , ouabain , chemistry , atpase , central nervous system , binding site , size exclusion chromatography , endogeny , chromatography , biochemistry , enzyme , adsorption , sodium , endocrinology , biology , organic chemistry
Endogenous inhibitors of Na,K‐ATPase and ouabain‐binding were partially purified from bovine central nervous system, and some of their properties were studied. They were eluted as low‐molecular‐weight fractions by gel filtration. They could be adsorbed by both Amberlite IR 120 and Amberlite IRA 400 at acidic and basic pH, respectively, indicating that they could act as both anions and cations at different pH. These inhibitors of ouabain‐binding appeared to affect specific binding of ouabin, and Scatchard plot analysis showed that the in hibition was competitive, suggesting that they could bind to the same site as ouabain, presumably to Na,K‐ATPase itself. The inhibitory activities were heat stable, but charring inactivated them completely.