Peptic hydrolysis of ovalbumin modified by acetylation,
dc.contributor.author | Neuhaus, Otto W. | en_US |
dc.contributor.author | Miller, Lila | en_US |
dc.date.accessioned | 2006-04-13T15:03:38Z | |
dc.date.available | 2006-04-13T15:03:38Z | |
dc.date.issued | 1957-09 | en_US |
dc.identifier.citation | Neuhaus, 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.uri | http://www.sciencedirect.com/science/article/B6WB5-4DW2P64-2TC/2/520dcce7261d7f179dd743bb7f8eecd7 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/32500 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=13459438&dopt=citation | en_US |
dc.description.abstract | 1. 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.extent | 466177 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 | Peptic hydrolysis of ovalbumin modified by acetylation, | en_US |
dc.type | Article | en_US |
dc.rights.robots | IndexNoFollow | en_US |
dc.subject.hlbsecondlevel | Public Health | en_US |
dc.subject.hlbsecondlevel | Chemistry | en_US |
dc.subject.hlbsecondlevel | Chemical Engineering | en_US |
dc.subject.hlbsecondlevel | Biological Chemistry | en_US |
dc.subject.hlbtoplevel | Engineering | en_US |
dc.subject.hlbtoplevel | Science | en_US |
dc.subject.hlbtoplevel | Health Sciences | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | Department of Biological Chemistry, Medical School, University of Michigan, Ann Arbor, Michigan, USA; Dept. of Anatomy, Wayne State University, Detroit, Mich. | en_US |
dc.contributor.affiliationum | Department of Biological Chemistry, Medical School, University of Michigan, Ann Arbor, Michigan, USA | en_US |
dc.identifier.pmid | 13459438 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/32500/1/0000587.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1016/0003-9861(57)90018-8 | en_US |
dc.identifier.source | Archives of Biochemistry and Biophysics | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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