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1.
J Indian Med Assoc ; 2002 Oct; 100(10): 619
Article Dans Anglais | IMSEAR | ID: sea-105023

Résumé

An evaluation of clinical efficacy of nizer versus nimesulide tablets was undertaken in 118 patients suffering from otitis media. Nizer demonstrated rapid and powerful analgesic and antipyretic effects compared to plain nimesulide, without additional side effects.


Sujets)
Adolescent , Adulte , Anti-inflammatoires non stéroïdiens/effets indésirables , Enfant , Cyclodextrines/effets indésirables , Inhibiteurs des cyclooxygénases/effets indésirables , Association médicamenteuse , Études d'évaluation comme sujet , Femelle , Humains , Mâle , Adulte d'âge moyen , Otite moyenne/complications , Douleur/traitement médicamenteux , Sulfonamides/effets indésirables , Facteurs temps , Résultat thérapeutique , Cyclodextrines bêta
2.
Indian J Pediatr ; 1999 Mar-Apr; 66(2): 290-3
Article Dans Anglais | IMSEAR | ID: sea-78998

Résumé

Research has shown that anticonvulsants are teratogens and pose a risk for fetal malformations. Though Fetal Hydantoin Syndrome (FHS) was first reported by Langhman and others, wide phenotypic variability of this syndrome has lead many clinicians to question its very existence. We report a twelve year old girl with FHS with rheumatic valvular heart disease.


Sujets)
Malformations dues aux médicaments et aux drogues/étiologie , Anticonvulsivants/effets indésirables , Enfant , Femelle , Anomalies morphologiques congénitales de la main/induit chimiquement , Humains , Déficience intellectuelle/induit chimiquement , Ongles malformés/induit chimiquement , Phénytoïne/effets indésirables , Rhumatisme cardiaque/complications , Syndrome
3.
Indian J Biochem Biophys ; 1993 Feb; 30(1): 36-41
Article Dans Anglais | IMSEAR | ID: sea-26459

Résumé

The elution profile of the core sequence enzymes of the phenyl propanoid pathway, namely phenyl alanine ammonia lyase, t-cinnamic acid 4-hydroxylase and p-coumaryl CoA ligase, on AcA 34 column suggested the existence of a high molecular form (P1) and a low molecular form (P2) for all the three enzymes. All the P1 forms eluted together in same fractions, while the P2 forms eluted out according to their respective molecular mass. Rechromatography of P1 form under identical conditions showed a similar elution profile (Q1 and Q2 forms). Further, the Q1 form did not show any significant increase in specific activity when compared to the P1 form. These results suggested the possibility of these enzymes existing as a protein cluster. Further confirmation was obtained on repeated column chromatography of the Q1 form in presence of 0.1 M KCl which did not result in complete dissociation of the complex to its individual enzyme components. The identification of the subunit polypeptide of the individual enzyme components in the multi enzyme complex and the in vitro demonstration of the phenyl propanoid core pathway reaction sequence using phenylalanine alone as a substrate supplementing the required cofactors for appropriate reactions substantiated that at least the core enzymes of the phenyl propanoid sequence existed as a multi enzyme complex.


Sujets)
Coenzyme A ligases/isolement et purification , Cytochrome P-450 enzyme system/isolement et purification , Mixed function oxygenases/isolement et purification , Complexes multienzymatiques/isolement et purification , Phenylalanine ammonia-lyase/isolement et purification , Plantes/enzymologie , Solanum tuberosum/enzymologie , Trans-cinnamate 4-monooxygenase
4.
Indian J Biochem Biophys ; 1992 Oct; 29(5): 418-24
Article Dans Anglais | IMSEAR | ID: sea-27787

Résumé

The cytoplasmic localisation of cinnamic acid 4-hydroxylase (CA4H) has been shown by isolation and subcellular fractionation of the enzyme in Hepes buffer. The enzyme was purified by ammonium sulphate fractionation followed by AcA-34 molecular sieve chromatography. The enzyme existed as a high molecular mass which dissociated to a lower form on dilution on the column. The pH optimum, sulphydryl requirement, molecular and preliminary kinetic characteristics were investigated.


Sujets)
Cations divalents , Fractionnement cellulaire , Cytochrome P-450 enzyme system/isolement et purification , Concentration en ions d'hydrogène , Cinétique , Microsomes/enzymologie , Mixed function oxygenases/isolement et purification , Solanum tuberosum/enzymologie , Fractions subcellulaires/enzymologie , Trans-cinnamate 4-monooxygenase
5.
Indian J Biochem Biophys ; 1991 Jun; 28(3): 193-7
Article Dans Anglais | IMSEAR | ID: sea-28876

Résumé

The change in activity of cinnamic acid 4-hydroxylase (CA4H) in potato parenchyma tissue exposed to various conditions has been examined. Maximum induction of CA4H activity was obtained at 18 hr of incubation. Though CA4H induction can occur in dark, over 100% increase in enzyme activity was obtained on exposure of the tissue to light. Actinomycin D and cycloheximide inhibited the induction process. Mn2+, though known to cause an induction of CA4H in Jerusalem Artichoke, strongly inhibited potato CA4H induction. Dithiothreitol enhanced the CA4H activity due to either activation or protection of the enzyme. CA4H induction was significantly regulated at very low concentrations of trans-cinnamate and paracoumarate.


Sujets)
Cycloheximide/pharmacologie , Cytochrome P-450 enzyme system/biosynthèse , Dactinomycine/pharmacologie , Obscurité , Dithiothréitol/pharmacologie , Induction enzymatique , Cinétique , Lumière , Mixed function oxygenases/biosynthèse , Solanum tuberosum/enzymologie , Trans-cinnamate 4-monooxygenase
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