Human hand impedance characteristics during maintained posture

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

Purification and characterization of macrolide 2''-phosphotransferase type II from a strain of Escherichia coli highly resistant to macrolide antibiotics

Hyperimmune and high-titered polyclonal pneumococcal antisera, specific for cross-reactive types within groups, were produced in adult rabbits. Purified capsular polysaccharide was injected intravenously into adult rabbits. One week later, these rabbits were given multiple intravenous injections of formalin-inactivated pneumococci of the cross-reactive type by an established method. Each of the resultant antisera were specific for the cross-reactive type indicating that the previous injection of the polysaccharide had induced epitope-specific tolerance. This method was successful for production of antisera against pneumococcal types 6A, 6B, 9N, 9V, 19F and 19A. Polyclonal rabbit pneumococcal antisera have some advantages over murine monoclonal antibodies for serologic studies and this method should be applicable for producing type-specific antibodies to cross-reactive polysaccharides of clinical interest. Further, this method is simpler and generally produces higher titered monovalent (factor) reagents than absorbed antisera.     

Modelling and analyzing density-dependent population processes: Comparison between wild and laboratory strains of the bean weevil,Callosobruchus chinensis (L.)

Three models were constructed for analyzing the population characteristics ofC. chinensis on stored beans; model A describing the whole reproductive process with a single equation, model B describing the three age-specific processes (oviposition, egg survival and larval survival) with separate equations, and model C which describes all these processes not for the whole habitat but for the individual beans comprizing it. The logit equation was employed here as a common basis to describe the density-response relationship involved. All three models showed very good fit to the experimental data obtained for both laboratory and wild strains of the weevil. The parameter values characterizing the population dynamics were, however, widely different between the two strains; the laboratory one which had been reared for some 500 generations showed significantly higher reproductive capacity, less sensitive and gentler response to crowding in both adult and egg stages, and more uniform egg distribution among individual beans, as compared with the wild strain newly introduced. Sensitivity analyses using these models suggested that these changes in population characteristics have been attained by the process of domestication or adaptation to stable laboratory conditions through a long period of time. This process seemed in effect to have optimized the population's performances in the laboratory environment. Evolutionary significance of such optimization was discussed with reference to the selection pressure which may have acted upon individuals.     

Purification of hepatitis B virus gene X product synthesized in Escherichia coli and its detection in a human hepatoblastoma cell line producing hepatitis B virus

A fused gene containing 94% of the hepatitis B virus (HBV) open reading frame X was expressed in Escherichia coli, and its 17-kDa product was purified by ion-exchange chromatography. Antibody elicited against the X-gene product reacted with materials proximal to the nuclear membrane of a human hepatoblastoma cell line producing HBV particles. No such reaction was observed with the same cell line that did not produce HBV particles.     

The role of the tryptophyl residue in the hypotensive peptide xenopsin

The role of the Trp⁶ residue in the biological activity of the hypotensive peptide xenopsin (<Glu-Gly-Lys-Arg-Pro-Trp-Ile-Leu-OH) was investigated. This residue was satisfactorily reduced to 2,3-dihydro-Trp on treatment with excess pyridine-borane in trifluoroacetic acid without any detectable change in other parts of the molecule. The analogous peptide, (Lys², Gly³) xenopsin, was also reduced in a similar manner. Both reduction products were purified by gel filtration and characterized by UV absorption, amino acid composition, and structural analysis.The reduced peptides were assayed on the fundus strip of isolated rat stomach and were found to possess less than 1 percent of the activity of the original peptides. Although each of the reduced analogs had an indoline substituted for an indole in the tryptophyl residue, their biological activity was virtually lost. This suggests that the tryptophyl residue of xenopsin is crucial for its biological activity.     

A soluble enzyme activity that attaches free diaminopimelic acid to bdelloplast peptidoglycan

An enzyme activity, responsible for the attachment of diaminopimelic acid (DAP) to bdelloplast wall peptidoglycan, was studied in an in vitro, cell-free system. Most of the activity was found in the high-speed (20000g) supernatant fraction of homogenates of bdelloplasts prepared from a culture of the intracellular bacterium Bdellovibrio bacteriovorus 109J, growing synchronously within cells of Escherichia coli. Peptidoglycan preparations obtained either from E. coli ML35 or from the walls of bdelloplasts synchronously cultured for 40 or 90 min served as the acceptors in this reaction, whereas cell wall or peptidoglycan preparations obtained from Gram-positive bacteria could not function as acceptors of DAP. The attachment activity had an apparent Km value for DAP of 10 microM; for bdelloplast peptidoglycan, it was approximately 0.43 mg/mL, which is 13 microM with respect to peptidoglycan disaccharide peptide units. DAP attachment was partially inhibited by the structural analogues lanthionine, L-ornithine, beta-aminobutyric acid, and D-serine, as well as the cell wall synthesis inhibitors penicillin G, ampicillin, and cephalexin. This enzyme activity is present only during the intracellular stage of the bdellovibrio's developmental growth cycle and may serve a stage-specific function of biochemically modifying the cell in which it grows.