| Literature DB >> 16615854 |
E I Goufman1, S A Moshkovskii, O V Tikhonova, P G Lokhov, V G Zgoda, M V Serebryakova, I Yu Toropygin, M A Vlasova, M R Safarova, O V Makarov, A I Archakov.
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.Entities:
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Year: 2006 PMID: 16615854 DOI: 10.1134/s000629790604002x
Source DB: PubMed Journal: Biochemistry (Mosc) ISSN: 0006-2979 Impact factor: 2.487