Title : Comparison of inactivation and unfolding of methanol dehydrogenase during denaturation in guanidine hydrochloride and urea.

Pub. Date : 2000 Aug

PMID : 10940644






2 Functional Relationships(s)
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1 The activity and the conformational changes of methanol dehydrogenase (MDH), a quinoprotein containing pyrrolo-quinoline quinone as its prosthetic group, have been studied during denaturation in guanidine hydrochloride (GdnHCl) and urea. PQQ Cofactor malate dehydrogenase 2 Homo sapiens
2 The activity and the conformational changes of methanol dehydrogenase (MDH), a quinoprotein containing pyrrolo-quinoline quinone as its prosthetic group, have been studied during denaturation in guanidine hydrochloride (GdnHCl) and urea. PQQ Cofactor malate dehydrogenase 2 Homo sapiens