Studies on the active center of D- and L-lactate dehydrogenases using oxamate-diaminohexyl-sepharose affinity chromatography [Limulus polyphemus]

Vertebrate and invertebrate L-lactate dehydrogenases (L-lactate:NAD+ oxidoreductase, EC 1.1.1.27) are effectively bound to oxamate-diaminohexyl-Sepharose, whereas several D-lactate dehydrogenases (D-lactate:NAD+ oxidoreductase, EC 1.1.1.28) do not bind to the same Sepharose. One explanation for our...

Ausführliche Beschreibung

Gespeichert in:

Bibliographische Detailangaben
Veröffentlicht in:	Proceedings of the National Academy of Sciences - PNAS 1980-10, Vol.77 (10), p.5832-5836
Hauptverfasser:	Tuengler, P, Stein, T.N, Long, G.L
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Binding Sites Biochemistry Chromatography Chromatography, Affinity - methods Dehydrogenases Elution Enzymes Horseshoe crabs Horseshoe Crabs - enzymology Isoenzymes Isomerism L-Lactate Dehydrogenase - metabolism Lobsters Molecules Nephropidae Polysaccharides - metabolism Sepharose - analogs & derivatives Sepharose - metabolism Substrate Specificity Sulfates Vertebrates
Online-Zugang:	Volltext
Tags:	Tag hinzufügen Keine Tags, Fügen Sie den ersten Tag hinzu!

Beschreibung
Zusammenfassung:	Vertebrate and invertebrate L-lactate dehydrogenases (L-lactate:NAD+ oxidoreductase, EC 1.1.1.27) are effectively bound to oxamate-diaminohexyl-Sepharose, whereas several D-lactate dehydrogenases (D-lactate:NAD+ oxidoreductase, EC 1.1.1.28) do not bind to the same Sepharose. One explanation for our findings is that the enzymes' substrate is oriented in a reversed manner in the active center of the D- and L-lactate dehydrogenases.
ISSN:	0027-8424 1091-6490
DOI:	10.1073/pnas.77.10.5832