Studies on phosphodeoxyribomutase
dc.contributor.author | Smith, Charles G. | en_US |
dc.contributor.author | Bernstein, Isadore A. | en_US |
dc.date.accessioned | 2006-04-13T14:57:03Z | |
dc.date.available | 2006-04-13T14:57:03Z | |
dc.date.issued | 1961-09-02 | en_US |
dc.identifier.citation | Smith, Charles G., Bernstein, I. A. (1961/09/02)."Studies on phosphodeoxyribomutase." Biochimica et Biophysica Acta 52(1): 184-193. <http://hdl.handle.net/2027.42/32351> | en_US |
dc.identifier.uri | http://www.sciencedirect.com/science/article/B73G9-486T547-NY/2/b2c975eb555c41af865013ffc9284c14 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/32351 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=13914169&dopt=citation | en_US |
dc.description.abstract | A phosphodeoxyribomutase has been demonstrated in cell-free extracts of Sarcina lutea. The enzyme could be heated to 55[deg] for at least 2 h and still retain activity. It had a pH optimum around 7.2, and the most highly purified preparation showed a specific activity of approx. 60 [mu]moles of deoxyribose 1-phosphate converted to deoxyribose 5-phosphate/mg protein/h. The enzyme was constitutive in the above organism, but could not be demonstrated conclusively in extracts of 14 other microorganisms tested.The enzymic conversion of deoxyribose 1-phosphate to deoxyribose 5-phosphate was established by isolation and enzymic characterization of the product. The enzyme was also able to convert deoxyribose 5-phosphate to pyrimidine-bound deoxyribose, presumably through deoxyribose 1-phosphate. Chromatographic and radiographic studies indicated that, at equilibrium, the reaction contains approx. 95% deoxyribose 5-phosphate and 5% deoxyribose 1-phosphate.The mutase was shown to be inhibited by inorganic phosphate at low concentrations, and by deoxyribose 1-phosphate, deoxyribose 5-phosphate, potassium sulfate and fructose 6-phosphate. The enzyme appeared to be stimulated by fructose 1,6-diphosphate. The inhibitions by inorganic phosphate and sulfate confirm previous reports in the literature.Acetaldehyde and an aqueous extract of Whatman No. 1 filter paper were shown to interfere with the cysteine-sulfuric acid reaction with deoxyribose. | en_US |
dc.format.extent | 747031 bytes | |
dc.format.extent | 3118 bytes | |
dc.format.mimetype | application/pdf | |
dc.format.mimetype | text/plain | |
dc.language.iso | en_US | |
dc.publisher | Elsevier | en_US |
dc.title | Studies on phosphodeoxyribomutase | en_US |
dc.type | Article | en_US |
dc.rights.robots | IndexNoFollow | en_US |
dc.subject.hlbsecondlevel | Materials Science and Engineering | en_US |
dc.subject.hlbsecondlevel | Chemistry | en_US |
dc.subject.hlbsecondlevel | Chemical Engineering | en_US |
dc.subject.hlbtoplevel | Science | en_US |
dc.subject.hlbtoplevel | Engineering | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | Department of Dermatology and the Institute of Industrial Health, University of Michigan, Ann Arbor, Mich., U.S.A.; Research Laboratories, The Upjohn Company, Kalamazoo, Mich., U.S.A. | en_US |
dc.contributor.affiliationum | Department of Dermatology and the Institute of Industrial Health, University of Michigan, Ann Arbor, Mich., U.S.A.; Research Laboratories, The Upjohn Company, Kalamazoo, Mich., U.S.A. | en_US |
dc.identifier.pmid | 13914169 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/32351/1/0000422.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1016/0006-3002(61)90916-7 | en_US |
dc.identifier.source | Biochimica et Biophysica Acta | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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