The development of small entrepreneurship in Russia

The paper summarises the findings of field research projects on emerging Russian entrepreneurship carried out by the author over a six-year period. The main stages of small and medium enterprise (SME) formation in Russia since the late 1980s are considered. Then, the dynamics of the SME sector are analysed, using available official statistics. Major market entry problems are reviewed, followed by an analysis of the institutional system for the development and support of SMEs. Specific issues of SME involvement in the informal/shadow economy are reviewed. Finally, the most recent trends in small entrepreneurship development are considered. The study offers answers to the following challenging questions: How has the profile of small entrepreneurship changed within the last decade? Why did expansion of the SME sector stop in the mid-1990s after dramatic increases during the early years of the decade? Are the administrative and economic barriers to market entry becoming stronger or weaker for small entrepreneurs? What are the outcomes of the policies and measures intended to build up a system of institutional support for SMEs? To what extent are small enterprises involved in the informal economy? How did the August 1998 financial crisis affect the SME sector? Both quantitative and qualitative data are used for tackling these issues on a national and regional level, and particular emphasis is given to the Tomsk region. – entrepreneurship ; private sector ; SME ; transitio

The Development of Small Entrepreneurship in Russia

Entrepreneurship, Private sector, SME, Transition

Characterization of the ligand binding site of the bovine IgA Fc receptor (bFcαR)

Recently, we identified a bovine IgA Fc receptor (bFcαR), which shows high homology to the human myeloid FcαR, CD89. IgA binding has previously been shown to depend on several specific residues located in the B-C and F-G loops of the membrane-distal extracellular domain 1 of CD89. To compare the ligand binding properties of these two FcαRs, we have mapped the IgA binding site of bFcαR. We show that, in common with CD89, Tyr-35 in the B-C loop is essential for IgA binding. However, in contrast to earlier observations on CD89, mutation of residues in the F-G loop did not significantly inhibit IgA binding.</p

The Solution Structures of Two Human IgG1 Antibodies Show Conformational Stability and Accommodate Their C1q and FcγR Ligands.

The human IgG1 antibody subclass shows distinct properties compared with the IgG2, IgG3, and IgG4 subclasses and is the most exploited subclass in therapeutic antibodies. It is the most abundant subclass, has a half-life as long as that of IgG2 and IgG4, binds the FcγR receptor, and activates complement. There is limited structural information on full-length human IgG1 because of the challenges of crystallization. To rectify this, we have studied the solution structures of two human IgG1 6a and 19a monoclonal antibodies in different buffers at different temperatures. Analytical ultracentrifugation showed that both antibodies were predominantly monomeric, with sedimentation coefficients s20,w (0) of 6.3-6.4 S. Only a minor dimer peak was observed, and the amount was not dependent on buffer conditions. Solution scattering showed that the x-ray radius of gyration Rg increased with salt concentration, whereas the neutron Rg values remained unchanged with temperature. The x-ray and neutron distance distribution curves P(r) revealed two peaks, M1 and M2, whose positions were unchanged in different buffers to indicate conformational stability. Constrained atomistic scattering modeling revealed predominantly asymmetric solution structures for both antibodies with extended hinge structures. Both structures were similar to the only known crystal structure of full-length human IgG1. The Fab conformations in both structures were suitably positioned to permit the Fc region to bind readily to its FcγR and C1q ligands without steric clashes, unlike human IgG4. Our molecular models for human IgG1 explain its immune activities, and we discuss its stability and function for therapeutic applications