Polynucleotide Phosphorylase from a Cyanobacterium (Synechococcus sp.): Subunit Composition and Properties

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Nolden, W.-T.; Richter, G.: Polynucleotide Phosphorylase from a Cyanobacterium (Synechococcus sp.): Subunit Composition and Properties. In: Zeitschrift für Naturforschung - Section C Journal of Biosciences 37 (1982), Nr. 7-8, S. 600-608. DOI: https://doi.org/10.1515/znc-1982-7-809

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Abstract: 
Polynucleotide phosphorylase from cells of the cyanobacterium Synechococcus sp. has been purified 1400-fold by an improved procedure. The enzyme purified to homogeneity and lacking nuclease, phosphatase and protease contaminations reveals a single band of ADP polymerizing activity upon polyacrylamide gel electrophoresis under nondenaturing conditions which corresponds to a molecular mass of about 275 000. The enzyme migrates as a single polypeptide of Mr≈70 000 when subjected to gel electrophoresis in the presence of dodecyl sulfate indicating a composition of α4 for the native enzyme molecule. The isoelectric point of the purified enzyme as determined by isoelectric focusing was found to be at 4.2±0.1. Polynucleotide phosphorylase of Synechococcus is preferentially activated by Mg2+; Kcl has a significant stimulatory effect. © 1982, Walter de Gruyter. All rights reserved.
License of this version: CC BY-NC-ND 3.0
Document Type: article
Publishing status: publishedVersion
Issue Date: 1982
Appears in Collections:Naturwissenschaftliche Fakultät

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1 image of flag of Germany Germany 20 95.24%
2 image of flag of Algeria Algeria 1 4.76%

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