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Effect of xenon, nitrous oxide and halothane on membrane‐bound sialidase from calf brain
Author(s) -
Sandhoff K.,
Schraven J.,
Nowoczek G.
Publication year - 1976
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(76)80076-2
Subject(s) - physics , nitrous oxide , combinatorics , mathematics , chemistry , organic chemistry
Substances like xenon, nitrous oxide and halothane interact with proteins or membranes: xenon can be bound to hydrophobic regions of myoglobin [l] . Under hyperbaric pressures xenon, as well as nitrous oxide inhibit enzymes like tyrosinase, a-chymotrypsin and acetylcholinesterase [2]. On the other hand, halothane increases the fluidity of lipid membranes [3,4]. We studied the influence of these substances on membrane-bound sialidase which, together with its ganglioside and glycoprotein substrates, is found in neuronal membranes and mostly in the plasma membrane of nerve endings [5,6]. Unexpectedly we found an increase of particulate sialidase activity in the presence of higher concentrations of these substances when measured both on endogenous substrates as well as on the tritiumlabelled ganglioside GDIa*, added to the reaction mixture. This ganglioside is split by the enzyme into sialic acid and ganglioside G,, [7,8]. In this paper we report the first observation of an increase in enzyme activity as a result of the addition of xenon, nitrous oxide and halothane. Other membrane-bound enzymes (5’-nucleotidase, adenyl cyclase and Na’-K’ATPase) studied were slightly inhibited under comparable conditions.