UDP-glucosyltransferase activity of housefly microsomal fraction

Morello, Antonio; Repetto, Yolanda

doi:10.1042/bj1770809

Cited by 25 publications

(12 citation statements)

References 7 publications

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“…Also manganese and calcium can act as bivalent cation activators for UDP-glucosyltransfcrase of rat liver 191. Digitonin has been reportcd to activate rat liver UDPglucosyltransferase 2.5-fold towards bilirubin [9]. Also Triton X-I00 stimulates glucosidation of p-nitrophenol in the housefly preparation [15]. In our study neither sodium cholate nor sonication activated UDPglucosyltransferase in the microsomes of Leucoplzaea maderue fat body.…”

Section: Discussioncontrasting

confidence: 37%

“…The pH optima of UDPglucosyltransferase from different animal sources are generally broad and lie near 7 or are slightly alkaline [7, 9, 171. The activation of UDPglucosyltransferase by magnesium is evident. The optimal concentration, 10 mM for microsomal enzyme of P. ur?7ericuna, is of the same magnitude as for other substrates and species [9,15,211. Also manganese and calcium can act as bivalent cation activators for UDP-glucosyltransfcrase of rat liver 191. Digitonin has been reportcd to activate rat liver UDPglucosyltransferase 2.5-fold towards bilirubin [9].…”

Section: Discussionmentioning

confidence: 99%

“…Usually, after the termination of the reaction, protein is precipitated and laborious extractions are performed. The disappcarance of substrate or the production of glucoside is then determincd either by spectrophotometric [15,161 or fluorimetric 1161 methods. Radiometric methods using steroids, isoflavones and phenols as substrates have also been described [5,8,14,171.…”

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confidence: 99%

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UDPglucosyltransferase and Its Kinetic Fluorimetric Assay

Väisänen¹,

Mackenzie

Hänninen³

1983

European Journal of Biochemistry

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A rapid, Kinetic assay for UDPglucosyltransferase has been developed using 1‐naphthol as substrate. It is based on the continuous fluorimetric monitoring of 1‐naphthyl glucoside formation during the reaction at physiological pH. The conjugate is easily distinguished from aglycone, since their fluorimetric properties differ. Glucoside biosynthesis in vitro by microsomal preparations isolated from the gut and fat body of cockroaches Periplaneta americana and Leucophaea maderae, and from the green gland and hepatopancreas of the crayfish Astacus astacus, has been demonstrated. The effects of buffer, pH, MgCl2, UDP‐glucuronic acid, UDP‐N‐acetylglucosamine, sodium cholate and sonication on the enzyme activity have been assessed. The kinetic parameters of 1‐naphthol and UDP‐glucose have also been determined.

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Section: Discussioncontrasting

confidence: 37%

Section: Discussionmentioning

confidence: 99%

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confidence: 99%

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UDPglucosyltransferase and Its Kinetic Fluorimetric Assay

Väisänen¹,

Mackenzie

Hänninen³

1983

European Journal of Biochemistry

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“…UDPGT activity was determined according to Morello and Repetto (1979) as modiWed by Leszczynski et al (1992). The reaction mixture consisted of 1 ml of the aphid supernatant, 0.833 mM UDP-glucose, 0.167 mM p-nitrophenol, 16.7 mM MgCl 2 , and 0.8% Triton X-100 buVered to pH 7.5.…”

Section: Preparation Of the Enzymesmentioning

confidence: 99%

Effect of host plant alternation on some adaptive enzymes of the bird cherry–oat aphid, Rhopalosiphum padi (L.)

Łukasik¹

2008

J Pest Sci

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Changes in the activity of some adaptive enzymes of the bird cherry-oat aphid R. padi after transfer from primary (bird cherry) to secondary (triticales) host plants were assessed. The following groups of enzymes were studied: (1) transferases-glutathione S-transferase (GST) and UDP-glucosyltransferase (UDPGT); (2) antioxidant enzymes-superoxide dismutase (SOD) and catalase (CAT); (3) oxidoreductases-polyphenol oxidase (PPO) and peroxidase (PX); and (4) glucoside hydrolases--and -glucosidase. The activity of the transferases and the antioxidant enzymes increased after transfer to the secondary host, but the level of activity was closely associated with feeding duration on the secondary host. The strongest induction was noted for SOD, the activity of which was more than three times greater on the secondary than on the primary host. In contrast, transfer of the bird cherry-oat aphid was accompanied by a decline in activity of PPO, PX, and -glucosidase; PPO and PX activity was 50% less in aphids fed on the secondary host rather than on the primary host. Activity of -glucosidase increased after prolonged feeding on the secondary host. The results indicated that the adaptive enzymes of the bird cherry-oat aphid enable it to feed on distantly related host plants.

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“…In insects, the glycosylation of small lipophilic compounds has been considered as a minor enzymatic detoxification mechanism for half a century (Ahmad et al, 1986;Brattsten, 1988;Després et al, 2007;Smith, 1962). Insect UGT enzyme activity has been investigated in the housefly Musca domestica (Morello and Repetto, 1979), in the fruitfly Drosophila melanogaster (Real et al, 1991), in the tobacco hornworm Manduca sexta (Ahmad and Hopkins, 1992), in the silkworm Bombyx mori , and in other insects (Ahmad and Hopkins, 1993b). These biochemical studies have shown that the insect UGT enzymes typically use UDP-glucose as the main sugar donor unlike vertebrate UGTs which mainly utilize UDP-glucuronic acid.…”

Section: Introductionmentioning

confidence: 98%