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Govorun V.M.,RAS Shemyakin Ovchinnikov Institute of Bioorganic Chemistry | Ivanov V.T.,Scientific Research Institute of Physicochemical Medicine
Russian Journal of Bioorganic Chemistry | Year: 2011

The review is focused on topical issues of biomedical proteomics and peptidomics. Modern pro teomic techniques used in medical studies-extraction, detection and obtained data processing-have been given a lot of attention. The means of applying chromatographic, mass-spectrometric, and chromatographic mass-spectrometric methods in proteogenomic and biomedical studies as well as during biomarker searches are discussed in detail. © 2011 Pleiades Publishing, Ltd.

Polyakov N.B.,RAS Shemyakin Ovchinnikov Institute of Bioorganic Chemistry | Slizhikova D.K.,RAS Shemyakin Ovchinnikov Institute of Bioorganic Chemistry | Izmalkova M.Y.,RAS Shemyakin Ovchinnikov Institute of Bioorganic Chemistry | Cherepanova N.I.,RAS Shemyakin Ovchinnikov Institute of Bioorganic Chemistry | And 7 more authors.
Biochemistry (Moscow) | Year: 2010

Intact chloroplasts were prepared from protoplasts of the moss Physcomitrella patens according to an especially developed method. They were additionally separated into stroma and thylakoid fractions. The proteomes of intact plastids, stroma, and thylakoids were analyzed by 1D-electrophoresis under denaturing conditions followed by protein digestion and nano-LC-ESI-MS/MS of tryptic peptides from gel bands. A total of 624 unique proteins were identified, 434 of which were annotated as chloroplast resident proteins. The majority of proteins belonged to a photosynthetic group (21.3%) and to the group of proteins implicated in protein degradation, posttranslational modification, folding, and import (20.6%). Among proteins assigned to chloroplasts, the following groups are prominent combining proteins implicated in metabolism of: amino acids (6.9%), nucleotides (2.5%), lipids (2.2%), carbohydrates (2.4%), hormones (1.5%), isoprenoids (1.25%), vitamins and cofactors (1%), sulfur (1.25%), and nitrogen (1%); as well as proteins involved in the pentose-phosphate cycle (1.75%), tetrapyrrole synthesis (3.7%), and redox processes (3.6%). The data can be used in physiological and photobiological studies as well as in further studies of P. patens chloroplast proteome including structural and functional specifics of plant protein localization in organelles. © 2010 Pleiades Publishing, Ltd.

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