Human hand impedance characteristics during maintained posture

Received: 23 June 1993 / Accepted in revised form: 15 September 1994     

A direct evidence of the localization of mitochondrial calmodulin

The presence and localization of mitochondrial calmodulin was directly proved immuno-electron microscopically by the protein A-gold technique. In the ultra-pure mitochondria the complexes of anti-calmodulin antibody and protein A-gold clearly showed the localization of mitochondrial calmodulin on the inner membrane and in the matrix space.     

High-performance anion-exchange chromatography of ultraviolet-absorbing constituents of human urine

A 100-μl urine sample was chromatographed on a column packed with a strongly basic macroreticular anion-exchange resin (Diaion CDR-10, 5– μm diameter with a nominal 35% cross linkage). The elution was performed with a linear acetate gradient from 0 to 6.0 M at an average flow-rate of 0.72 ml/min and at an average pressure of 104 kg/cm². The relative standard deviation of retention times and peak height was ± 4% or less. The properties of the macroreticular anion-exchange resin, the effect of the particle size, the pH of acetate buffers, and the effect of the flow-rate of the eluent on the separation were investigated. Thirty three components of urine were then resolved and named.     

Targeting Interleukin-6: All the Way to Treat Autoimmune and Inflammatory Diseases

Interleukin (IL)-6, a cytokine featuring redundancy and pleiotropic activity, contributes to host defense against acute environmental stress, while dysregulated persistent IL-6 production has been demonstrated to play a pathological role in various autoimmune and chronic inflammatory diseases. Targeting IL-6 is thus a rational approach to the treatment of these diseases. Indeed, clinical trials of tocilizumab, a humanized anti-IL-6 receptor antibody have verified its efficacy and tolerable safety for patients with rheumatoid arthritis, Castleman''s disease and systemic juvenile idiopathic arthritis, resulting in approval of this innovative biologic for treatment of these diseases. Moreover, a considerable number of case reports and pilot studies of off-label use of tocilizumab point to the beneficial effects of tocilizumab for a variety of other phenotypically different autoimmune and chronic inflammatory diseases. Elucidation of the source of IL-6 and of mechanisms through which IL-6 production is dysregulated can thus be expected to lead to clarification of the pathogenesis of various diseases.     

Enzyme localization and orientation of the active site of dissimilatory nitrite reductase from Bacillus firmus

The location of the dissimilatory nitrite reductase and orientation of its reducing site of the Grampositive denitrifier, Bacillus firmus NIAS 237 were examined. Approximately 90% of the total dissimilatory nitrite reductase activity with ascorbate-reduced phenazine methosulfate (PMS) as the electron donor was on the protoplast membrane. Nitrite induced with intact Bacillus cells an alkalinization in the external medium, followed by acidification. The electron transfer inhibitor, 2-heptyl-4-hydroxyquinoline-N-oxide, which blocked nitrite reduction with endogenous substrates, inhibited the acidification, but not the alkalinization. Alkalinization was not affected with ascorbate-reduced PMS as the artificial electron donor. This indicated that the alkalinization is not associated with proton consumption outside the cytoplasmic membrane by the extracellular nitrite reduction. The dissimilatory nitrite reductase of B. firmus NIAS 237 was located on the cytoplasmic membrane, and its reducing site is suggested to be on the inner side of this membrane.Abbreviations CCCP carbonylcyanide m-chlorophenylhydrazone - HOQNO 2-heptyl-4-hydroxyquinoline-N-oxide - PMS phenazine methosulfate - H⁺/NO _inf2 ^sup- ratio number of consumed protons in the external medium per one ion of NO _inf2 ^sup- reduced     

Molecular characterization of an adenylate cyclase gene of the cyanobacterium Spirulina platensis

A cyaA gene, encoding an adenylate cyclase, was isolated from a filamentous cyanobacterium, Spirulina platensis, by functional complementation of a cya mutant of Escherichia coli, defective in adenylate cyclase activity. The predicted gene product of cyaA contains a signal peptide-like domain, a putative sensor domain similar to the gene product of vsrA of Pseudomonas solanacearum, a putative membrane-spanning domain and an adenylate cyclase-like catalytic domain. Two other positive clones that complemented the E. coli mutant were isolated from the same cyanobacterium, suggesting that several cya genes are functioning in S. platensis.