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Action of phloridzine and various glycosides on mammalian trehalases

J. Labat, J. F. Demelier, and J. E. Courtois

Laboratoires de biochimie de VHôpital Laennec et de la Faculté de phmmacie, Paris

 

Abstract: The intestinal trehalase of pig has been purified. Its properties are similar to those of purified tréhalases from the kidneys of man or pig: optimum pH about 5.7, trehalose —trehalase linkage dissociated little, absence of activation by metal cations, competitive inhibition by sucrose. Some phenol hétérosides have manifested inhibition: phloridzine, arbutino, piceoside. Phloretol causes a more important inhibition in comparison to phloridzine. Among the hétérosides with a structure resembling that of phloridzine which have been studied, only isoasebotine and salipurposide have proved to be inhibitors. The possible physiological role of these tréhalases is discussed in connection with the results obtained.

Full paper in Portable Document Format: 2310a776.pdf (in French)

 

Chemical Papers 23 (10) 776–786 (1969)

Tuesday, July 23, 2024

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