ABSTRACT
The eEF1 family of mammalian translation elongation factors is comprised of the two variants of eEF1A (eEF1A1 and eEF1A2), and the eEF1B complex. The latter consists of eEF1Bα, eEF1Bß, and eEF1Bγ subunits. The two eEF1A variants have similar translation activity but may differ with respect to their secondary, "moonlighting" functions. This variability is underlined by the difference in the spatial organization of eEF1A1 and eEF1A2, and also possibly by the differences in their post-translational modifications. Here, we review the data on the spatial organization and post-translation modifications of eEF1A1 and eEF1A2, and provide examples of their involvement in various processes in addition to translation. We also describe the structural models of eEF1B subunits, their organization in the subcomplexes, and the trimeric model of the entire eEF1B complex. We discuss the functional consequences of such an assembly into a complex as well as the involvement of individual subunits in non-translational processes.
ABSTRACT
Pegylated interferon alpha-2b (PEG-IFN alpha-2b) is a domestic preparation of a modified recombinant interferon alpha-2b with prolonged effect. The preparation was obtained by N-terminal pegylation of IFN alpha-2b with polyethylene glycol (PEG). This paper presents the method of PEG-IFN alpha-2b synthesis and characteristics of the obtained product. PAAG electrophoresis, Western blot analysis and MALDI-TOF mass-spectrometry confirm that the preparation is an N-terminal pegylated IFN alpha-2b that contains no more than 10% of dipegylated IFN alpha-2b. The comparison of PEG-IFN alpha-2b with its foreign analogue has revealed the similarity of their biological activity and pharmacokinetic parameters.
Subject(s)
Antiviral Agents/chemistry , Antiviral Agents/pharmacology , Interferon-alpha/chemistry , Interferon-alpha/pharmacology , Technology, Pharmaceutical/methods , Animals , Antiviral Agents/administration & dosage , Antiviral Agents/blood , Antiviral Agents/isolation & purification , Cattle , Cell Line , Cytopathogenic Effect, Viral/drug effects , Delayed-Action Preparations , Drug Carriers/chemistry , Humans , Interferon alpha-2 , Interferon-alpha/administration & dosage , Interferon-alpha/blood , Interferon-alpha/isolation & purification , Models, Molecular , Polyethylene Glycols , Rats , Rats, Wistar , Recombinant Proteins , Spectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationABSTRACT
The photosynthetic membrane composition and low temperature fluorescence spectra were analyzed for pea chloroplasts from control and clinostated plants. Clinorotation induces a decrease in the amount of the oligomeric form of the light-harvesting chlorophyll a/b complex (LHCII) and an increase of its monomeric form. Some changes in organization of photosystem 1 (PS1) complex were revealed as well. These changes are in accordance with the variations of fluorescence characteristics and photochemical activity.
