Abstract
The purification of a chromatin-bound antizyme to ornithine decarboxylase from germinated barley seeds is described. This antizyme was extracted from chromatin by 2M NaCl and purified to homogeneity. Its molecular weight was found to be 9000 with an isoelectric point of 4.1. It reacts with both cytosolic and chromatin- bound ornithine decarboxylase from generated barley seeds and E. coli but it does not inhibit ornithine decarboxylase of Tetrahymena pyriformis or rat liver.
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© 1985 Martinus Nijhoff/Dr W. Junk Publishers, Dordrecht
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Panagiotidis, C.A., Kyriakidis, D.A. (1985). Purification of a non-histone protein with properties of antizyme to ornithine decarboxylase from germinated barley seeds. In: Galston, A.W., Smith, T.A. (eds) Polyamines in Plants. Advances in Agricultural Biotechnology, vol 18. Springer, Dordrecht. https://doi.org/10.1007/978-94-009-5171-6_4
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DOI: https://doi.org/10.1007/978-94-009-5171-6_4
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