Isolation, Purification, and Characterization of Aldolase from Human Heart

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Description

Aldolase from human heart has been purified 128-fold to a final specific activity of 11.52 units per mg. The purification procedure employed column chromatography on phosphocellulose.

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71 leaves : ill.

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Allen, Benja L. August 1972.

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This thesis is part of the collection entitled: UNT Theses and Dissertations and was provided by the UNT Libraries to the UNT Digital Library, a digital repository hosted by the UNT Libraries. It has been viewed 189 times. More information about this thesis can be viewed below.

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  • Allen, Benja L.

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Description

Aldolase from human heart has been purified 128-fold to a final specific activity of 11.52 units per mg. The purification procedure employed column chromatography on
phosphocellulose.

Physical Description

71 leaves : ill.

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UNT Theses and Dissertations

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  • August 1972

Added to The UNT Digital Library

  • June 4, 2013, 10:29 p.m.

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  • Dec. 12, 2013, 10:42 a.m.

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Allen, Benja L. Isolation, Purification, and Characterization of Aldolase from Human Heart, thesis, August 1972; Denton, Texas. (https://digital.library.unt.edu/ark:/67531/metadc163995/: accessed March 28, 2024), University of North Texas Libraries, UNT Digital Library, https://digital.library.unt.edu; .

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