dc.identifier.uri | http://dx.doi.org/10.15488/2464 | |
dc.identifier.uri | http://www.repo.uni-hannover.de/handle/123456789/2490 | |
dc.contributor.author | Nolden, W.-T. | |
dc.contributor.author | Richter, G. | |
dc.date.accessioned | 2017-11-24T11:46:31Z | |
dc.date.available | 2017-11-24T11:46:31Z | |
dc.date.issued | 1982 | |
dc.identifier.citation | 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 | |
dc.description.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. | eng |
dc.language.iso | eng | |
dc.publisher | Berlin : De Gruyter | |
dc.relation.ispartofseries | Zeitschrift für Naturforschung - Section C Journal of Biosciences 37 (1982), Nr. 7-8 | |
dc.rights | CC BY-NC-ND 3.0 Unported | |
dc.rights.uri | https://creativecommons.org/licenses/by-nc-nd/3.0/ | |
dc.subject | Affinity Chromatography | eng |
dc.subject | Isoelectric Focusing | eng |
dc.subject | Poly(A) Synthesis | eng |
dc.subject | Polyacrylamide Gel Electrophoresis | eng |
dc.subject | Tetrameric Structure | eng |
dc.subject.ddc | 570 | Biowissenschaften, Biologie | ger |
dc.title | Polynucleotide Phosphorylase from a Cyanobacterium (Synechococcus sp.): Subunit Composition and Properties | |
dc.type | Article | |
dc.type | Text | |
dc.relation.essn | 1865-7125 | |
dc.relation.issn | 0939-5075 | |
dc.relation.doi | https://doi.org/10.1515/znc-1982-7-809 | |
dc.bibliographicCitation.issue | 7-8 | |
dc.bibliographicCitation.volume | 37 | |
dc.bibliographicCitation.firstPage | 600 | |
dc.bibliographicCitation.lastPage | 608 | |
dc.description.version | publishedVersion | |
tib.accessRights | frei zug�nglich |
The following license files are associated with this item: