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1.
J Pharm Bioallied Sci ; 4(3): 231-5, 2012 Jul.
Artículo en Inglés | MEDLINE | ID: mdl-22923966

RESUMEN

OBJECTIVE: to investigate the hepatoprotective potential of ether insoluble phenolic components of n-butanol fraction (EPC-BF) of flaxseed against CCl(4) -induced liver damage in rats. MATERIALS AND METHODS: Hepatotoxicity was induced to Wistar rats by administration of 0.2% CCl(4) in olive oil (8 mL/kg, i.p.) on the seventh day of treatment. Hepatoprotective potential of EPC-BF at doses, 250 and 500 mg/kg, p.o. was assessed through biochemical and histological parameters. RESULTS: EPC-BF and silymarin pretreated animal groups showed significantly decreased activities of Aspartate aminotransferase (AST), alanine aminotransferase (ALT), alkaline phosphatase (ALP), and level of total bilirubin, elevated by CCl(4) intoxication. Hepatic lipid peroxidation elevated by CCl(4) intoxication were also found to be alleviated at almost normal level in the EPC-BF and silymarin pretreated groups. Histological studies supported the biochemical findings and treatment of EPC-BF at doses 250 and 500 mg/kg, p.o. was found to be effective in restoring CCl(4) -induced hepatic damage. However, EPC-BF did not show dose-dependent hepatoprotective potential. EPC-BF depicted maximum protection against CCl(4) -induced hepatic damage at lower dose 250 mg/kg than higher dose (500 mg/ kg). CONCLUSION: EPC-BF possesses the significant hepatoprotective activity against CCl(4) induced liver damage, which could be mediated through increase in antioxidant defenses.

2.
Indian J Cancer ; 49(1): 181-7, 2012.
Artículo en Inglés | MEDLINE | ID: mdl-22842186

RESUMEN

BACKGROUND: Actin cytoskeleton is involved in actin-based cell adhesion, cell motility, and matrix metalloproteinases(MMPs) MMP2, MMP9, MMP11 and MMP14 are responsible for cell invasion in breast cancer metastasis. The dietary intake of lignan from flax seed gets converted to enterolactone (EL) and enterodiol in the human system. Here we show that the enterolactone has a very significant anti-metastatic activity as demonstrated by its ability to inhibit adhesion and invasion and migration in MCF-7 and MDA MB231 cell lines. MATERIALS AND METHODS: Migration inhibition assay, actin-based cell motility assay along with reverse transcriptase polymerase chain reaction (RT-PCR) for MMP2, MMP9, MMP11 and MMP14 genes were performed in MCF-7 and MDA MB 231 cell lines. RESULTS: Enterolactone seems to inhibit actin-based cell motility as evidenced by confocal imaging and photo documentation of cell migration assay. The results are supported by the observation that the enterolactone in vitro significantly down-regulates the metastasis-related metalloproteinases MMP2, MMP9 and MMP14 gene expressions. No significant alteration in the MMP11 gene expression was found. CONCLUSIONS: Therefore we suggest that the anti-metastatic activity of EL is attributed to its ability to inhibit cell adhesion, cell invasion and cell motility. EL affects normal filopodia and lamellipodia structures, polymerization of actin filaments at their leading edges and thereby inhibits actin-based cell adhesion and cell motility. The process involves multiple force-generating mechanisms of actin filaments i.e. protrusion, traction, deadhesion and tail-retraction. By down-regulating the metastasis-related MMP2, MMP9 and MMP14 gene expressions, EL may be responsible for cell invasion step of metastasis.


Asunto(s)
4-Butirolactona/análogos & derivados , Adhesión Celular/efectos de los fármacos , Movimiento Celular/efectos de los fármacos , Lignanos/farmacología , Invasividad Neoplásica , 4-Butirolactona/farmacología , Citoesqueleto de Actina/efectos de los fármacos , Neoplasias de la Mama/dietoterapia , Neoplasias de la Mama/patología , Femenino , Lino/metabolismo , Regulación Neoplásica de la Expresión Génica/efectos de los fármacos , Humanos , Técnicas In Vitro , Lignanos/administración & dosificación , Lignanos/metabolismo , Células MCF-7 , Metaloproteinasas de la Matriz/genética , Metaloproteinasas de la Matriz/metabolismo , Metástasis de la Neoplasia
4.
World J Microbiol Biotechnol ; 8(1): 42-4, 1992 Jan.
Artículo en Inglés | MEDLINE | ID: mdl-24425332

RESUMEN

Glucose prevented maltose utilization in batch culture ofSaccharomyces cerevisiae whereas in a mixed carbohydrate-limited system, maltose and glucose were consumed simultaneously. The specific activity of α-glucosidase depended on the dilution rate as well as the proportion of maltose in the mixture. The chemostat provides a way of reaching the low residual concentrations of glucose in the broth that are necessary to release catabolite repression and permit maltose induction of α-glucosidase.

5.
Biochem Biophys Res Commun ; 111(3): 1105-12, 1983 Mar 29.
Artículo en Inglés | MEDLINE | ID: mdl-6301484

RESUMEN

Studies on the composition and characterization of DNA product(s) synthesized by calf thymus terminal deoxynucleotidyl transferase were performed using homopolymeric single-stranded, calf thymus double-stranded, and native DNA resident in calf thymus chromatin preparations as priming DNA species. Synthesis was carried out using equimolar concentrations of all four deoxynucleoside triphosphates as substrates and Mg2+ or Mn2+ as an effective divalent cation. Irrespective of the nature of the priming DNA or the divalent cation, the DNA product contained 60-70% dGMP residues, 10-15% each of the two pyrimidine residues, and 5-10% dAMP residues. The product synthesized using chromatin DNA as initiator was predominantly single-stranded and its synthesis was resistant to actinomycin D. The predilection of terminal deoxynucleotidyl transferase to synthesize dGMP-rich products on natural or homopolymeric DNA primers suggests that such products may represent biologically important recognition signal sequences.


Asunto(s)
ADN Nucleotidilexotransferasa/metabolismo , ADN Nucleotidiltransferasas/metabolismo , ADN/biosíntesis , Animales , Catálisis , Bovinos , Fenómenos Químicos , Química , Cromatina/metabolismo , Guanosina Monofosfato/aislamiento & purificación , Timo/enzimología
6.
Prep Biochem ; 9(1): 71-84, 1979.
Artículo en Inglés | MEDLINE | ID: mdl-155814

RESUMEN

A simple method for the preparation of sweet potato beta-amylase by thymol amylose adsorption is described. The method is far more efficient and gives higher recovery of the enzyme. The crystalline enzyme thus obtained is found to be homogeneous by gel chromatography, polyacrylamide gel electrophoresis.


Asunto(s)
Amilasas/aislamiento & purificación , Plantas/enzimología , beta-Amilasa/aislamiento & purificación , Adsorción , Sulfato de Amonio , Amilosa/análogos & derivados , Cromatografía en Gel , Cristalización , Electroforesis en Gel de Poliacrilamida , Precipitación Fraccionada , Métodos , Peso Molecular , Timol
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