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Biochemistry (Mosc) ; 71(4): 354-60, 2006 Apr.
Article in English | MEDLINE | ID: mdl-16615854

ABSTRACT

One of the problems of plasma proteomics is a presence of large major components. In this work, we use the thermostable fraction as a way to deplete these major proteins. The thermostable fraction of serum samples from patients with ovarian, uterus, and breast cancers and benign ovarian tumor was analyzed using two-dimensional electrophoresis combined with MALDI-TOF(-TOF)-mass spectrometry. Of them, alpha-1-acid glycoprotein and clusterin are expressly down-regulated in breast cancer, whereas transthyretin is decreased specifically in ovarian cancer. Apolipoprotein A-I forms have decreased spot volumes, while haptoglobin alpha1, in contrast, is elevated in several tumors. These data are partly consistent with previous art studies on cancer proteomics, which involve mass-spectrometry-based serum profiling techniques. Serum thermostable fraction may be recommended as a good tool for medium and small protein proteome investigation, in particular, by 2D-electrophoresis.


Subject(s)
Biomarkers, Tumor/blood , Electrophoresis, Gel, Two-Dimensional/methods , Neoplasm Proteins/blood , Proteome/analysis , Proteomics/methods , Adult , Aged , Breast Neoplasms/blood , Breast Neoplasms/metabolism , Female , Humans , Middle Aged , Ovarian Neoplasms/blood , Ovarian Neoplasms/metabolism , Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization , Uterine Neoplasms/blood , Uterine Neoplasms/metabolism
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