THE EFFECTS OF OXYGEN ON FERMENTATION IN GIARDIA-LAMBLIA

被引：47

作者：

PAGET, TA ^{[1
]}

KELLY, ML ^{[1
]}

JARROLL, EL ^{[1
]}

LINDMARK, DG ^{[1
]}

LLOYD, D ^{[1
]}

机构：

[1] UNIV WALES COLL CARDIFF,PABIO,MICROBIOL GRP,CARDIFF,WALES

来源：

MOLECULAR AND BIOCHEMICAL PARASITOLOGY | 1993年 / 57卷 / 01期

基金：

英国惠康基金;

关键词：

GIARDIA-LAMBLIA; FERMENTATION; NAD(P)H FLUORESCENCE; REDOX; GLUTAMATE DEHYDROGENASE; ALANINE AMINOTRANSFERASE;

D O I：

10.1016/0166-6851(93)90244-R

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Detailed study of the effects of oxygen on the carbohydrate metabolism of Giardia lamblia revealed that low concentrations of oxygen ( < 0.25 muM) produced profound alterations in the carbon balance of this organism. Although this concentration of oxygen could not be detected by mass spectrometry, a marked stimulation of ethanol production was observed. Associated with this was an inhibition of alanine production and oxidation of the intracellular NAD(P)H pool. Higher concentrations of oxygen inhibited ethanol production and further reduced levels of alanine. These results suggest that this stimulation is due to changes in carbon flux. Analysis of cell and medium hydrolysates after the growth of trophozoites in [U-C-14]glucose suggests that G. lamblia does not synthesise detectable levels of labelled amino acids, except alanine and to a lesser extent valine, from this sugar. Trophozoites of G. lamblia have both glutamate dehydrogenase and alanine aminotransferase activity. As glutamate is taken up from the medium, it is suggested that glutamate dehydrogenase and alanine aminotransferase cooperate to convert pyruvate to alanine, with the concomitant oxidation of NAD(P)H.

引用

页码：65 / 72

页数：8

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