Purification and some properties of isocitrate dehydrogenase of a blowfly Aldrichina grahami |
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| Institution: | 1. Department of Biomedical Sciences, University of Padova, IT-35131 Padova, Italy;2. Biochemistry & Biomedicine, School of Life Sciences, University of Sussex, Brighton BN1 9QG, UK;3. Faculty of Medicine and Health Technology, FI-33014 Tampere University, Finland;4. Department of Cardiothoracic Surgery, Center for Sepsis Control and Care (CSCC), Jena University Hospital, DE-07747 Jena, Germany;1. American University of Beirut Medical Center, Pathology and Laboratory Medicine Department, Cairo Street, Hamra, Beirut, Lebanon;2. Université Paris Cité, Inserm, Maladies neurodéveloppementales et neurovasculaires, F-75019 Paris, France;3. Faculty of Medicine and Health Technology, FI-33014, Tampere University, Finland;4. Institute of Biotechnology, University of Helsinki, Helsinki, Finland |
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| Abstract: | - 1.1. NADH-dependent isocitrate dehydrogenase has been purified 110-fold from the crude extract of the flight muscle mitochondria of Aldrichina grahami.
- 2.2. The purification procedure involved Triton X-100 treatment of isolated mitochondria, column chromatography on DEAE-cellulose, Affi-gel blue, and P-cellulose.
- 3.3. The purified enzyme was homogeneous by criteria of the polyacrylamide gel electrophoresis.
- 4.4. The enzyme of the blowfly contains more acidic amino acids and less hydrophobic amino acids than that of pig heart.
- 5.5. The molecular weight was determined to be 330,000 daltons. The subunit construction differs from ghat of mammalian isocitrate dehydrogenase.
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