Methanol detoxification by enzyme-loaded erythrocytes.
Alcohol oxidase (AlOx) from Pichea pastoris (a methylotrophic yeast) was encapsulated into human and murine erythrocytes up to 2 units/ml of packed cells. This enzyme has a much higher affinity for methanol than for ethanol, thus making the loaded erythrocytes useful cellular bioreactors able to catabolize methanol. Enzyme-loaded erythrocytes showed an increased rate of the hexose-monophosphate-shunt activity and a significant methaemoglobin production. However, the in vivo survival of these cells does not seem to be significantly affected by methanol catabolism. In vivo, mice receiving AlOx-loaded erythrocytes were able to keep the blood methanol concentrations below values that were about 50% of those found in mice receiving unloaded cells and similar amounts of methanol. Thus AlOx-loaded erythrocytes may add an important contribution to the detoxification protocol against methanol poisoning.
Magnani
M
M
Istituto di Chimica Biologica G. Fornaini, Università degli Studi, Urbino (PS), Italy.
Fazi
A
A
Mangani
F
F
Rossi
L
L
Mancini
U
U
D000429:Alcohol Oxidoreductases / Q000378:metabolism*; D000818:Animals; D004905:Erythrocyte Aging; D004912:Erythrocytes / Q000201:enzymology*; D000431:Ethanol / Q000378:metabolism / Q000633:toxicity; D006801:Humans; D000432:Methanol / Q000378:metabolism* / Q000633:toxicity; D008706:Methemoglobin / Q000096:biosynthesis; D051379:Mice; D010843:Pichia / Q000201:enzymology
D000431:Ethanol; D008706:Methemoglobin; D000429:Alcohol Oxidoreductases; C019643:alcohol oxidase; D000432:Methanol