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An alkaline phosphomonoesterase from Neurospora crassa
dc.contributor.authorKuo, Mau-Huaien_US
dc.contributor.authorBlumenthal, Harold J.en_US
dc.date.accessioned2006-04-13T14:56:45Z
dc.date.available2006-04-13T14:56:45Z
dc.date.issued1961-11-25en_US
dc.identifier.citationKuo, Mau-Huai, Blumenthal, Harold J. (1961/11/25)."An alkaline phosphomonoesterase from Neurospora crassa." Biochimica et Biophysica Acta 54(1): 101-109. <http://hdl.handle.net/2027.42/32344>en_US
dc.identifier.urihttp://www.sciencedirect.com/science/article/B73G9-486T4B1-CP/2/f6f942f18bfa85c975c698e37de545ceen_US
dc.identifier.urihttps://hdl.handle.net/2027.42/32344
dc.identifier.urihttp://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=14460640&dopt=citationen_US
dc.description.abstractAn alkaline phosphomonoesterase was purified 40-fold from mycelium of Neurospora crassa. The enzyme had a pH maximum of 8.9-9.0 with [beta]-glucerol phosphate as substrate and exhibited maximal activity in the presnece of Mg2+. The enzyme was nearly completely resolved with respect to its Mg2+ requirement and was very sensitive to inhibition with Be2+. The substrate specificity of the enzyme was studied using 21 compounds and the properties of the enzyme were compared with those of the acid phosphomonoesterase previously isolated from the same organism.en_US
dc.format.extent537868 bytes
dc.format.extent3118 bytes
dc.format.mimetypeapplication/pdf
dc.format.mimetypetext/plain
dc.language.isoen_US
dc.publisherElsevieren_US
dc.titleAn alkaline phosphomonoesterase from Neurospora crassaen_US
dc.typeArticleen_US
dc.rights.robotsIndexNoFollowen_US
dc.subject.hlbsecondlevelMaterials Science and Engineeringen_US
dc.subject.hlbsecondlevelChemistryen_US
dc.subject.hlbsecondlevelChemical Engineeringen_US
dc.subject.hlbtoplevelScienceen_US
dc.subject.hlbtoplevelEngineeringen_US
dc.description.peerreviewedPeer Revieweden_US
dc.contributor.affiliationumDepartment of Bacteriology, The University of Michigan Medical School, Ann Arbor, Mich., U.S.A.en_US
dc.contributor.affiliationumDepartment of Bacteriology, The University of Michigan Medical School, Ann Arbor, Mich., U.S.A.en_US
dc.identifier.pmid14460640en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/32344/1/0000414.pdfen_US
dc.identifier.doihttp://dx.doi.org/10.1016/0006-3002(61)90942-8en_US
dc.identifier.sourceBiochimica et Biophysica Actaen_US
dc.owningcollnameInterdisciplinary and Peer-Reviewed


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