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Peptic hydrolysis of ovalbumin modified by acetylation,

dc.contributor.authorNeuhaus, Otto W.en_US
dc.contributor.authorMiller, Lilaen_US
dc.date.accessioned2006-04-13T15:03:38Z
dc.date.available2006-04-13T15:03:38Z
dc.date.issued1957-09en_US
dc.identifier.citationNeuhaus, Otto W., Miller, Lila (1957/09)."Peptic hydrolysis of ovalbumin modified by acetylation,." Archives of Biochemistry and Biophysics 71(1): 162-169. <http://hdl.handle.net/2027.42/32500>en_US
dc.identifier.urihttp://www.sciencedirect.com/science/article/B6WB5-4DW2P64-2TC/2/520dcce7261d7f179dd743bb7f8eecd7en_US
dc.identifier.urihttps://hdl.handle.net/2027.42/32500
dc.identifier.urihttp://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=13459438&dopt=citationen_US
dc.description.abstract1. 1. Two types of acetylated ovalbumin derivatives designated as N-and N,O-acetylovalbumin were prepared by treatment with ketene at pH's 5.6 and 9.0, respectively.2. 2. Both limited and extensive acetylation decreases the digestibility of ovalbumin by crystalline pepsin.3. 3. The limited digestion of the N,O-acetylovalbumin may be attributed to three influences: the acetyl groups on the seven amino groups unsubstituted in the N-acetyl derivative, those on the tyrosyl residues, and those in unidentified positions, rather than to any one of these.4. 4. The results are in agreement with the view that pepsin is of broad specificity toward protein substrates.en_US
dc.format.extent466177 bytes
dc.format.extent3118 bytes
dc.format.mimetypeapplication/pdf
dc.format.mimetypetext/plain
dc.language.isoen_US
dc.publisherElsevieren_US
dc.titlePeptic hydrolysis of ovalbumin modified by acetylation,en_US
dc.typeArticleen_US
dc.rights.robotsIndexNoFollowen_US
dc.subject.hlbsecondlevelPublic Healthen_US
dc.subject.hlbsecondlevelChemistryen_US
dc.subject.hlbsecondlevelChemical Engineeringen_US
dc.subject.hlbsecondlevelBiological Chemistryen_US
dc.subject.hlbtoplevelEngineeringen_US
dc.subject.hlbtoplevelScienceen_US
dc.subject.hlbtoplevelHealth Sciencesen_US
dc.description.peerreviewedPeer Revieweden_US
dc.contributor.affiliationumDepartment of Biological Chemistry, Medical School, University of Michigan, Ann Arbor, Michigan, USA; Dept. of Anatomy, Wayne State University, Detroit, Mich.en_US
dc.contributor.affiliationumDepartment of Biological Chemistry, Medical School, University of Michigan, Ann Arbor, Michigan, USAen_US
dc.identifier.pmid13459438en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/32500/1/0000587.pdfen_US
dc.identifier.doihttp://dx.doi.org/10.1016/0003-9861(57)90018-8en_US
dc.identifier.sourceArchives of Biochemistry and Biophysicsen_US
dc.owningcollnameInterdisciplinary and Peer-Reviewed


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