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1.
Article | IMSEAR | ID: sea-203594

ABSTRACT

Background: Cellular glycosylation changes are associatedwith different types of neoplastic transformation. Fucose is adeoxyhexose sugar that the body requires for optimal functionsof cell to cell communications and which plays a role in severalbiological events. Fucose has been considered to play asignificant role in cancer and its spread. Alpha L Fucosidase(ALF) is an exoglycosidase involved in the hydrolyticdegradation of fucose containing components of glycoproteins,glycolipids and oligosaccharides. The significance of thisenzyme in human catabolism is implied by geneticneurovisceral storage disease. Altered levels of ALF has beenreported in the plasma/serum of patients with oral cancer.Aims: To investigate the clinical usefulness of serum fucoseand α-L-fucosidase in diagnosing oral pre-cancer and cancerand study the variations of the levels of both metabolites innormal, precancerous and cancerous conditions (Squamouscell carcinoma).Methodology: The study group comprised of 87 samples of(age range: 20-70 years): control samples – healthy individualswithout any systemic illness (n =20), clinically andhistopathologically diagnosed cases of leukoplakia (n=16) andoral submucous fibrosis (n=16) and oral squamous cellcarcinoma (n=35) respectively. 2ml blood was collected byvenipuncture from every subject after informed consent, serumwas separated and checked for fucose and fucosidase byspectrophotometric analysis.Results: The Normal value range of fucose is 8.3 to 9.5 mg/ dland that of fucosidase is 22.8 ± 7.1 U/L. There is an increasein the value range of fucose and fucosidase in the tissues ofpotentially malignant disorders and Squamous cell Carcinoma.

2.
Article in English | IMSEAR | ID: sea-158094

ABSTRACT

Proteins of the stress tolerant and mesophilic yeast were extracted using optimized protein extraction method and estimated by Bradford method. Immobilized pH gradient (IPG) strips were rehydrated with known concentrations of protein samples. Rehydrated IPG strips were run in isoelectric focusing (IEF) to separate the proteins on the basis of their pH gradient. 2DE gels were run, stained and image of the stress tolerant yeast was compared with the gel image of mesophilic yeast. The image analysis using the image master software resulted in the identification of differentially expressed spots in stress tolerant yeast. Among the differentially expressed spots, six were selected and characterized by MALDI-TOF as Enolase, Fructose bisphosphate aldolase, Alcohol dehydrogenase, 30KDa HSP, HSP70 and HSP90.

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