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1.
Arab Journal of Biotechnology. 2008; 11 (1): 39-46
en Inglés | IMEMR | ID: emr-85757

RESUMEN

Breast carcinoma ranks as first malignancy affecting females, contributing 33% of all female cancers. The C-erbB-2 is a class of oncogenes prevalent in breast cancer that play a role in cancer development. This research was performed to assess HER-2/neu oncogene amplification by semi-quantitative PCR technology, and HER-2/neu expression using immunohistochemical [IHC] staining. Electron microscopy made a contribution to the final diagnosis in the only case of invasive duct carcinoma. HER-2/neu gene amplification positive by PCR was detected in 40% of invasive duct breast cancer and showed a significant correlation between HER-2/neu gene amplification by PCR and HER-2/neu gene expression by IHC. Breast tumor specimens from 20 patients invasive duct carcinoma were studied; 10 without radiotherapy treatment and 10 after radiotherapy treatment. The study revealed a significant increase in chromosomal breaks and chromosomal rearrangements in breast cancer patients. There are also increases in chromosomal aberrations in patients received radiotherapy compared with patients not received radiotherapy. Cytogenetic study could be used as a prognostic factor in some breast cancer cases


Asunto(s)
Humanos , Femenino , Receptor ErbB-2 , Inmunohistoquímica , Microscopía Electrónica , Reacción en Cadena de la Polimerasa , Radioterapia , Aberraciones Cromosómicas , Análisis Citogenético
2.
Arab Journal of Biotechnology. 2007; 10 (2): 259-274
en Inglés | IMEMR | ID: emr-81825

RESUMEN

Seventeen local bacterial isolates which can hydrolyze a wide range of organophosphate [OP] insecticides were purified. They were reduced to ten different isolates based on their RAPD pattern and protein profile and termed as ASM-1 through ASM-10. Chemical assay and bioassay revealed that the isolate ASM-5 was the best isolate in chlorpyrifos degradation. The morphological and molecular identification characterized ASM-5 as Agrobacterium tumefaciens. A gene encoding a protein involved in OP hydrolysis was cloned and sequenced from A. tumefaciens ASM-5. This gene [named opdA] had sequence similarity about 98.7% with the A. tumefaciens opd gene. The coding sequence of the gene was sub cloned down stream an inducible expression promoter to evaluate the gene-enzyme system responsible for its OP-hydrolyzing activity. The biological activity of OPDA protein became more efficient compared to OPDA native protein


Asunto(s)
Insectos , Bioensayo , Proteínas Bacterianas , Reacción en Cadena de la Polimerasa , Clonación Molecular , Organofosfatos
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