Mingchun Xiao

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The mode of binding of myosin subfragment-1 (S1) to actin is known to depend on their molar ratio: when actin is in excess, S1 binds to two actin monomers within the actin filament, and when S1 is in excess or is equimolar with actin, each S1 binds to one actin monomer. Since in vertebrate striated muscle actin is in molar excess over myosin, we expect that(More)
Bifidobacteria assimilated raffinose about 4-fold more effectively than other intestinal bacteria, and α-galactosidase was active in all strains of Bifidobacteria tested. The enzyme activity of Bifidobacterium breve grown on raffinose was highly and specifically increased. Its activity was 30-fold higher than that of B. breve grown on glucose. Melibiose was(More)
Microglial cells, which are immunocompetent cells, are involved in all diseases of the central nervous system. During their activation in various diseases, a variety of soluble factors are released. In the present study, the correlation between cytokine levels and microglial cell migration in the course of retinal degeneration of Royal College of Surgeons(More)
The binding curve of myosin subfragment-1 (S1) to F-actin is not a simple hyperbola: at high concentrations of S1 the binding curve can be transformed into a linear plot ("normal" binding), but at small concentrations of S1 the binding complications deform the binding curve and produce nonlinear transforms ("anomalous" binding) [Andreev, O. A., & Borejdo,(More)
Cis-parinaric acid (PA) binds to a hydrophobic pocket formed between the heavy chain of myosin subfragment-1 (S1) and the 41-residue N-terminal of essential light chain 1 (A1). The binding is strong (Ka = 5.6 x 10(7) M-1) and rigid (polarization = 0.334). PA does not bind to myofibrils in which A1 has been extracted or replaced with alkali light chain 2(More)
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