Isolation, characterization and partial sequencing of cystine and thiol peptides of pig heart lipoamide dehydrogenase
dc.contributor.author | Matthews, Rowena Green | en_US |
dc.contributor.author | Arscott, L. David | en_US |
dc.contributor.author | Williams, Charles H., Jr. | en_US |
dc.date.accessioned | 2006-04-07T16:42:52Z | |
dc.date.available | 2006-04-07T16:42:52Z | |
dc.date.issued | 1974-11-25 | en_US |
dc.identifier.citation | Matthews, Rowena Green, Arscott, L. David, Williams, Jr., Charles H. (1974/11/25)."Isolation, characterization and partial sequencing of cystine and thiol peptides of pig heart lipoamide dehydrogenase." Biochimica et Biophysica Acta (BBA) - Enzymology 370(1): 26-38. <http://hdl.handle.net/2027.42/22230> | en_US |
dc.identifier.uri | http://www.sciencedirect.com/science/article/B73GH-47S137M-NH/2/86ea6af03d87e8ac17269b4e4e95be62 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/22230 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=4609485&dopt=citation | en_US |
dc.description.abstract | Pig heart lipoamide dehydrogenase (EC 1.6.4.3) contains ten half-cystines (as cysteic acid) per mole of enzyme bound FAD. Two of these are linked in an intrachain cystine which acts in concert with the flavin during catalysis. A peptic peptide containing this active center disulfide has been isolated and shown to have the sequence: Glu-Thr-Leu-Gly-Gly-Thr-Cys-Leu-Asn-Val-Gly-Cys-Ile-Pro-Ser (Lys, Ala, Leu). The enzyme also contains seven titratable thiols when either 5,5'-dithiobis (2-nitrobenzoic acid) or iodoacetate is used as titrant. Tryptic peptides containing alkylated thiols have been isolated and characterized by amino acid composition and by their positions in two-dimensional chromatography-electrophoresis. On the basis of map position and composition, the peptides containing thiols can be distinguished from one another. The results are compared with recent data of Brown and Perham (Brown, J. P. and Perham, R. N. (1974) Biochem. J. 138, 505-512) on the compositions and partial sequences of tryptic chymotryptic peptides containing half-cystines. The combined data associate nine of the ten half-cystines with unique compositions. | en_US |
dc.format.extent | 722676 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 | Isolation, characterization and partial sequencing of cystine and thiol peptides of pig heart lipoamide dehydrogenase | 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 | Veterans Administration Hospital and The Department of Biological Chemistry, The University of Michigan, Ann Arbor, Mich. 48105, U.S.A. | en_US |
dc.contributor.affiliationum | Veterans Administration Hospital and The Department of Biological Chemistry, The University of Michigan, Ann Arbor, Mich. 48105, U.S.A. | en_US |
dc.contributor.affiliationum | Veterans Administration Hospital and The Department of Biological Chemistry, The University of Michigan, Ann Arbor, Mich. 48105, U.S.A. | en_US |
dc.identifier.pmid | 4609485 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/22230/1/0000664.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1016/0005-2744(74)90028-X | en_US |
dc.identifier.source | Biochimica et Biophysica Acta | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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