Zobrazeno 1 - 10 of 21 pro vyhledávání: '"E. A. Noltmann"'
1
Use of AMS 14C Analysis in the Study of Problems in Aspartic Acid Racemization-Deduced Age Estimates on Bone
Autor: L A Payen, Christine Prior, P. E. Hare, E A Noltmann, Peter Slota, Paul Ennis, R. E. Taylor
Publikováno v: Radiocarbon. 28:539-546
Major discordances between AMS 14C- and aspartic acid racemization (AAR)-deduced age estimates on bone samples have led to an examination of factors other than time and temperature that can fundamentally influence the degree of racemization observed
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::270c661efc8b34b410a22b0773bb3b3d
https://doi.org/10.1017/s0033822200007694
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2
Glucose-6-phosphate isomerase
Autor: S. E. Marshall, A. Achari, R. H. Palmieri, E. A. Noltmann, Hilary Muirhead
Publikováno v: Philosophical transactions of the Royal Society of London. Series B, Biological sciences. 293(1063)
Glucose-6-phosphate isomerase (EC 5 . 3 .1 .9) is a dimeric enzyme of molecular mass 132000 which catalyses the interconversion of D-glucose-6-phosphate and D-fructose- 6-phosphate. The crystal structure of the enzyme from pig muscle has been determi
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::31ce4458dc277f227614a6cf76f37b8c
https://pubmed.ncbi.nlm.nih.gov/6115414
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3
Isolation and sequence determination of two pyridoxal 5'-phosphate-labeled thermolysin peptides from pig muscle phosphoglucose isomerase
Autor: R H, Palmieri, D M, Gee, E A, Noltmann
Publikováno v: The Journal of biological chemistry. 257(14)
Pig muscle phosphoglucose isomerase modified with pyridoxal 5'-phosphate under conditions that cause at least 90% inactivation of its catalytic activity was found to incorporate about 1.5 eq of pyridoxal 5'-phosphate per subunit. After digestion with
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::09d99291390c85550b2805072baf678f
https://pubmed.ncbi.nlm.nih.gov/6211448
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4
The enediolate analogue 5-phosphoarabinonate as a mechanistic probe for phosphoglucose isomerase
Autor: J M, Chirgwin, E A, Noltmann
Publikováno v: The Journal of biological chemistry. 250(18)
A stable analogue has been prepared of the enediolate anion believed to occur transiently in the reaction of phosphoglucose isomerase. This compound, 5-phosphoarabinonate, is the strongest known competitive inhibitor of the enzyme (Ki = 3 times 10(-7
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::7c2911c46ad2e7eecd3515a94fe0aa8c
https://pubmed.ncbi.nlm.nih.gov/240821
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6
Mechanistic implications of the pH independence of inhibition of phosphoglucose isomerase by neutral sugar phosphates
Autor: J M, Chirgwin, T F, Parsons, E A, Noltmann
Publikováno v: The Journal of biological chemistry. 250(18)
In contrast to the strongly pH-dependent inhibition of phosphoglucose isomerase by substrate analogues with a free carboxyl group, inhibition of this enzyme by neutral sugar phosphates is essentially invariant between pH 7 and 9. Competitive inhibiti
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::e8fe664090255508086ddb381dfa3244
https://pubmed.ncbi.nlm.nih.gov/240822
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