Studies on glucosaminidase. 2. Substrates for N-acetyl-beta-glucosaminidase.

نویسندگان

  • J Borooah
  • D H Leaback
  • P G Walker
چکیده

the oxygen uptake and acetoacetate oxidation when added alone or with fumarate, but not in the presence of a-oxoglutarate. The reasons for these differences are discussed. Anaerobically, relatively slight inhibitions of the reduction of acetoacetate were observed. 6. The oxidation of L( + )-p-hydroxybutyrate is inhibited by dinitrophenol, whereas that of the D(-)-form is not. This is related to the fact that only the L(+)-form requires conversion into the coenzyme A derivative. The differences in the behaviour of the Land D-forms towards dinitrophenol were used to examine the configuration of the P-hydroxybutyrate formed in sheep-heart muscle aerobically and anaerobically. In both cases the D-form only was found.

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عنوان ژورنال:
  • The Biochemical journal

دوره 78 1  شماره 

صفحات  -

تاریخ انتشار 1961