Purification and characterization of the mitochondrial F1 atpase from Sorghum

Sane, Aniruddha P. ; Sane, Vidhu A. ; Sane, Prafullachandra V. (1996) Purification and characterization of the mitochondrial F1 atpase from Sorghum Phytochemistry, 43 (3). pp. 561-564. ISSN 0031-9422

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Official URL: http://www.sciencedirect.com/science/article/pii/0...

Related URL: http://dx.doi.org/10.1016/0031-9422(96)00314-7

Abstract

Purification and kinetic analysis of the sorghum mitochondrial F1 ATPase was attempted in order to understand the behaviour of plant monocot F1 ATPases. The purified F1 ATPase consisted of 6 subunits viz. α , β , γ , δ ', δ and ε unlike other monocot F1 ATPases reported so far. The additional subunit designated as δ ' is larger in size than the δ subunit, unlike in other dicot ATPase preparations. The enzyme has a low specific activity and is markedly affected by anions like bicarbonate and sulphite and cations like Mg2+ and Mn2+. It shows no Ca2+ dependent ATPase activity and has a very low GTPase activity, compared with other plant ATPases. Comparison of the sorghum ATPase with ATPases from other members of Gramineae reveals differences in their characteristics within the same family.

Item Type:Article
Source:Copyright of this article belongs to Elsevier Science.
ID Code:45150
Deposited On:25 Jun 2011 05:50
Last Modified:25 Jun 2011 05:50

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