Literature DB >> 18170

A simple procedure for isolating adenosine triphosphatase from mitochondria.

Z Drahota, J Houstĕk.   

Abstract

A simple method for isolation of adenosine triphosphatase (EC 3.6.1.3) from mitochondria is described. The enzyme is released from mitochondrial Lubrol particles by drastic sonication and purified by gel filtration on Sepharose 6-B. The described procedure is effective in isolating adenosine triphosphatase from rat liver as it is from beef heart mitochondria. The enzyme isolated from beef heart has a specific activity of 120 mumol P/min per mg protein and enzyme isolated from rat liver has a specific activity of 70 mumol P/min per mg protein when measured as a release of inorganic phosphate.

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Year:  1977        PMID: 18170     DOI: 10.1016/0005-2728(77)90093-7

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  3 in total

1.  Purification and properties of the adenosine triphosphatase released from the liver mitochondrial membrane by chloroform.

Authors:  D D Tyler; P R Webb
Journal:  Biochem J       Date:  1979-02-15       Impact factor: 3.857

2.  Purification and properties of adenosine triphosphatase solubilized from beef heart mitochondria by chloroform.

Authors:  J Kopecký; J Houstĕk; Z Drahota
Journal:  Mol Cell Biochem       Date:  1977-12-29       Impact factor: 3.396

3.  Nitration of specific tyrosines in FoF1 ATP synthase and activity loss in aging.

Authors:  Virginia Haynes; Nathaniel J Traaseth; Sarah Elfering; Yasuko Fujisawa; Cecilia Giulivi
Journal:  Am J Physiol Endocrinol Metab       Date:  2010-02-16       Impact factor: 4.310

  3 in total

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