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- W1492701363 abstract "Après avoir montré l'existence, et décrit les propriétés catalytiques d'une activité ATPasique soluble dans les mitochondries du foie de rat [1, 2], nous avons étudié les propriétés immunologiques et structurales de l'une des deux formes moléculaires de l'enzyme : l'ATPase I. Nous avons préparé l'antisérum anti-ATPase I et avons pu montrer la pureté de notre préparation enzymatique par immunodiffusion et immunoélectrophorèse. Une méthode immunohistochimique nous a également confirmé la localisation de l'ATPase I au niveau de la fraction soluble mitochondriale. Le poids moléculaire de l'ATPase I déterminé par filtration sur Sephadex G 100 est de 18.400, par électrophorèse sur gel de polyacrylamide nous avons trouvé 18.600. Le pHi de l'ATPase I est de 7,2. La détermination de la composition en acides aminés indique un taux relativement élevé en acide aspartique, acide glutamique, sérine et glycocolle. En évaluant le nombre de résidus d'acide aminés par molécules d'ATPase I, on obtient un poids moléculaire de 17.000. L'acide aminé NH2 terminal est l'alanine. Les cartes peptidiques obtenues après coupure au bromure de cyanogène ou par la trypsine sont conformes au nombre de résidus méthionine ou lysine et arginine que nous avons trouvés dans la molécule d'ATPase I. L'ATPase I n'est pas une glycoprotéine. We described previously the existence of a soluble ATPase activity in rat liver mitochondria [1]. The purification and catalytic properties have been described [2]. In a continuation of these experiments, we have studied the immunologic and structural properties of one molecular form of this enzyme: ATPase I. We have prepared the antiserum anti-ATPase I and demonstrated the purity of our enzyme preparation by immunodiffusion and immunoelectrophoresis. An immunohistochemical method also confirmed the localization of ATPase I in the soluble fraction of mitochondria. The molecular weight of ATPase I was measured by G 100 Sephadex gel filtration and was found to be 18,400; electrophoresis on polyacrylamide gels gave a value of 18,600. The pHi of ATPase I was found to be 7,2. Amino acid analysis showed high amounts of aspartic acid, glutamic acid, serine and glycine. The molecular weight calculated from the total amino acid residues was found to be 17,000. Alanine is the NH2 terminal amino acid. The peptide maps obtained after degrading ATPase I with cyanogen bromide or trypsin are in accordance with the methionine, lysine and arginine residues we found in the ATPase I molecule. ATPase I does not appear to be a glycoprotein." @default.
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- W1492701363 date "1979-02-01" @default.
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- W1492701363 title "Studies of soluble rat liver mitochondrial acid ATPases" @default.
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- W1492701363 doi "https://doi.org/10.1016/s0300-9084(79)80441-1" @default.
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