Lactate Dehydrogenase of Hymenolepis Diminuta: Isolation and Characterization

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Lactate dehydrogenase was isolated in pure form from crude extract of the cestode Hymenoleois diminuta by heat treatment and column chromatography. The purified enzyme has a specific activity of 106 units per mg protein. The molecular weight of the purified protein was 75,000 as determined by Sephadex gel filtration and analytical ultracentrifugation. An equilibrium ultracentrifugation study suggests a subunit molecular weight of 39,000. From these data, a dimer form of the native enzyme is proposed.

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55 leaves: ill.

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Burke, William F. December 1971.

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  • Burke, William F.

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Lactate dehydrogenase was isolated in pure form from crude extract of the cestode Hymenoleois diminuta by heat treatment and column chromatography. The purified enzyme has a specific activity of 106 units per mg protein. The molecular weight of the purified protein was 75,000 as determined by Sephadex gel filtration and analytical ultracentrifugation. An equilibrium ultracentrifugation study suggests a subunit molecular weight of 39,000. From these data, a dimer form of the native enzyme is proposed.

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55 leaves: ill.

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  • December 1971

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  • Dec. 27, 2012, 10:03 p.m.

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  • Nov. 12, 2013, 11:12 a.m.

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Burke, William F. Lactate Dehydrogenase of Hymenolepis Diminuta: Isolation and Characterization, thesis, December 1971; Denton, Texas. (https://digital.library.unt.edu/ark:/67531/metadc131460/: accessed April 24, 2024), University of North Texas Libraries, UNT Digital Library, https://digital.library.unt.edu; .

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