Studies of Bovine Liver Glutamate Dehydrogenase by Analytical Affinity Chromatography on Immobilized AMP Analogs

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Fältnamn	Indikatorer	Metadata
000		02950naa a2200349 4500
001		oai:DiVA.org:lnu-615
003		SwePub
008		100401s1979 \| \|\|\|\|\|\|\|\|\|\|\|000 \|\|eng\|
024	7	a https://urn.kb.se/resolve?urn=urn:nbn:se:lnu:diva-6152 URI
024	7	a https://doi.org/10.1016/0003-9861(79)90639-82 DOI
040		a (SwePub)lnu
041		a engb eng
042		9 SwePub
072	7	a ref2 swepub-contenttype
072	7	a art2 swepub-publicationtype
100	1	a Brodelius, Peteru Department of Chemistry, Q-058, University of California at San Diego, La Jolla, California 92093, U.S.A4 aut0 (Swepub:lnu)nbrpe
245	1 0	a Studies of Bovine Liver Glutamate Dehydrogenase by Analytical Affinity Chromatography on Immobilized AMP Analogs
264	1	b Elsevier BV,c 1979
338		a print2 rdacarrier
520		a Bovine liver glutamate dehydrogenase has been studied by analytical affinity chromatography on two immobilized AMP analogs, i.e., N6-(6-aminohexyl)-AMP and 8-(6-aminohexyl)-amino-AMP. The existence of various enzyme-coenzyme and enzyme-effector complexes has been verified. Also the cooperative formation of two ternary complexes, i.e., glutamic dehydrogenase (GHD)-NADP-glutamate and GDH-ADP-leucine, has been shown. The results of this study have been rationalized by the “ligand exclusion theory.” which has been proposed for the regulation of the glutamic dehydrogenase. It has been shown that the active site and the ADP-binding effector site are oriented close to each other on the enzyme. Furthermore, the data suggest that the adenylic site is not identical to the nonactive coenzyme binding site. A mechanism based on electrostatic interactions is suggested for the cooperative binding of oxidized coenzyme and substrate. Dissociation constants for complexes between the enzyme and two coenzyme fragments (P-ADPR and 2′,5′-ADP) have been estimated.
650	7	a NATURVETENSKAPx Biologix Biokemi och molekylärbiologi0 (SwePub)106022 hsv//swe
650	7	a NATURAL SCIENCESx Biological Sciencesx Biochemistry and Molecular Biology0 (SwePub)106022 hsv//eng
653		a Biochemistry
653		a Biokemi
653		a Biokemi
653		a Biochemistry
700	1	a Kaplan, N O4 aut
710	2	a Department of Chemistry, Q-058, University of California at San Diego, La Jolla, California 92093, U.S.A4 org
773	0	t Archives of Biochemistry and Biophysicsd : Elsevier BVg 194:2, s. 449-456q 194:2<449-456x 0003-9861
856	4	u http://www.sciencedirect.com/science?_ob=ArticleURL&_aset=V-WA-A-W-D-MsSAYZW-UUA-U-AACVBCDYVU-AACAEBYZVU-EDVDUUBVY-D-U&_rdoc=6&_fmt=summary&_udi=B6WB5-4DV0897-18T&_coverDate=05%2F31%2F1979&_cdi=6701&_orig=search&_st=13&_sort=d&view=c&_acct=C000050221&_version=1&_urlVersion=0&_userid=10&md5=557acda7c8bc468877ce683d426916ady Länktext
856	4 8	u https://urn.kb.se/resolve?urn=urn:nbn:se:lnu:diva-615
856	4 8	u https://doi.org/10.1016/0003-9861(79)90639-8

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Av författaren/redakt...: Brodelius, Peter; Kaplan, N O

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NATURVETENSKAP: NATURVETENSKAP; och Biologi; och Biokemi och mole ...

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Av lärosätet: Linnéuniversitetet

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