Purification of rat-liver [gamma]-hydroxyglutamate transminase and its probable identity with glutamate-aspartate transminase
dc.contributor.author | Maitra, Umadas | en_US |
dc.contributor.author | Dekker, Eugene E. | en_US |
dc.date.accessioned | 2006-04-13T14:47:46Z | |
dc.date.available | 2006-04-13T14:47:46Z | |
dc.date.issued | 1964-03-09 | en_US |
dc.identifier.citation | Maitra, Umadas, Dekker, Eugene E. (1964/03/09)."Purification of rat-liver [gamma]-hydroxyglutamate transminase and its probable identity with glutamate-aspartate transminase." Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects 81(3): 517-532. <http://hdl.handle.net/2027.42/32138> | en_US |
dc.identifier.uri | http://www.sciencedirect.com/science/article/B73GF-47PGX1N-2K/2/39b6345c180b249c1171a86fd7e08e27 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/32138 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=14170323&dopt=citation | en_US |
dc.description.abstract | 1. 1. An enzyme which catalyzes the transamination of [gamma]-hydroxyglutamate has been purified over 300-fold from rat-liver homogenates.2. 2. The following observations strongly suggest that [gamma]-hydroxyglutamate transminase is identical with glutamate-aspartate transaminase (-aspartate: 2-oxo-glutarate aminotransferase, EC 2.6.1.1): a, at all stages of purification from either rat-liver or pig-heart extracts, the glutamate to [gamma]-hydroxyglutamate transminase ratios are not significantly different; b, transaminase activity for both substrates declines at the same rate during controlled heat denaturation of the purified rat-liver enzyme; c, transamination of [gamma]-hydroxyglutamate is strongly inhibited by either -glutamate or -aspartate; d, glutarate and maleate function as competitive inhibitors for either glutamate or [gamma]-hydroxyglutamate and determined K1 values for a given inhibitor are the same for either amino acid; and e, the purified rat-liver enzyme has the same pH-activity curve for both substrates.3. 3. The erythro- and threo-isomers of [gamma]-hydroxy--glutamate serve as substrates for both isozymes of the rat-liver enzyme as well as for the pig-heart enzyme, although the former isomer is a somewhat better substrate. The corresponding -diastereo-isomers are enzymically inactive.4. 4. With [gamma]-hydroxyglutamate, only [alpha]-ketoglutarate and oxaloacetate serve as amino group acceptors; pyruvate, [alpha]-ketobutyrate, and [beta]-phenylpyruvate are inactive.5. 5. Other [gamma]-substituted forms of glutamic acid, including [gamma]-methyleneglutamic acid and [gamma]-hydroxy-[gamma]-methylglutamic acid, are also active with the purified enzymes. | en_US |
dc.format.extent | 992995 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 | Purification of rat-liver [gamma]-hydroxyglutamate transminase and its probable identity with glutamate-aspartate transminase | 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 Biological Chemistry, University of Michigan, Ann Arbor. Mich., U.S.A. | en_US |
dc.contributor.affiliationum | Department of Biological Chemistry, University of Michigan, Ann Arbor. Mich., U.S.A. | en_US |
dc.identifier.pmid | 14170323 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/32138/1/0000191.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1016/0926-6569(64)90136-1 | en_US |
dc.identifier.source | Biochimica et Biophysica Acta | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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