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Life Science Research (life + science_research)
Selected AbstractsThe science commons in life science research: structure, function, and value of access to genetic diversityINTERNATIONAL SOCIAL SCIENCE JOURNAL, Issue 188 2006Robert Cook-Deegan Innovation in the life sciences depends on how much information is produced as well as how widely and easily it is shared. Policies governing the science commons , or alternative, more restricted informational spaces , determine how widely and quickly information is distributed. The purpose of this paper is to highlight why the science commons matters and to analyse its structure and function. The main lesson from our analysis is that both the characteristics of the physical resources (from genes to microbes, plants and animals) and the norms and beliefs of the different research communities , think of the Bermuda rules in the human genome case or the Belem declaration for bioprospecting , matter in the institutional choices made when organising the science commons. We also show that the science commons contributes to solving some of the collective action dilemmas that arise in the production of knowledge in Pasteur's Quadrant, when information is both scientifically important and practically applicable. We show the importance of two of these dilemmas for the life sciences, which we call respectively the diffusion,innovation dilemma (how readily innovation diffuses) and the exploration,exploitation dilemma (when application requires collective action). [source] Solid-phase biotinylation of antibodies,JOURNAL OF MOLECULAR RECOGNITION, Issue 3 2004Elizabeth Strachan Abstract Biotinylation is an established method of labeling antibody molecules for several applications in life science research. Antibody functional groups such as amines, cis hydroxyls in carbohydrates or sulfhydryls may be modified with a variety of biotinylation reagents. Solution-based biotinylation is accomplished by incubating antibody in an appropriate buffered solution with biotinylation reagent. Unreacted biotinylation reagent must be removed via dialysis, diafiltration or desalting. Disadvantages of the solution-based approach include dilution and loss of antibody during post-reaction purification steps, and difficulty in biotinylation and recovery of small amounts of antibody. Solid-phase antibody biotinylation exploits the affinity of mammalian IgG-class antibodies for nickel IMAC (immobilized metal affinity chromatography) supports. In this method, antibody is immobilized on a nickel-chelated chromatography support and derivitized on-column. Excess reagents are easily washed away following reaction, and biotinylated IgG molecule is recovered under mild elution conditions. Successful solid phase labeling of antibodies through both amine and sulfhydryl groups is reported, in both column and mini-spin column formats. Human or goat IgG was bound to a Ni-IDA support. For sulfhydryl labeling, native disulfide bonds were reduced with TCEP, and reduced IgG was biotinylated with maleimide,PEO2 biotin. For amine labeling, immobilized human IgG was incubated with a solution of NHS,PEO4 biotin. Biotinylated IgG was eluted from the columns using a buffered 0.2,M imidazole solution and characterized by ELISA, HABA/avidin assay, probing with a streptavidin,alkaline phosphatase conjugate, and binding to a monomeric avidin column. The solid phase protocol for sulfhydryl labeling is significantly shorter than the corresponding solution phase method. Biotinylation in solid phase is convenient, efficient and easily applicable to small amounts of antibody (e.g. 100,,g). Antibody biotinylated on-column was found to be equivalent in stability and antigen-recognition ability to antibody biotinylated in solution. Solid-phase methods utilizing Ni-IDA resin have potential for labeling nucleic acids, histidine-rich proteins and recombinant proteins containing polyhistidine purification tags, and may also be applicable for other affinity systems and labels. Copyright © 2004 John Wiley & Sons, Ltd. [source] Influence of obstetric factors on the yield of mononuclear cells, CD34+ cell count and volume of placental/umbilical cord bloodJOURNAL OF OBSTETRICS AND GYNAECOLOGY RESEARCH (ELECTRONIC), Issue 1 2010Atsuko Omori Abstract Aim:, Placental/umbilical cord blood (CB) has been used increasingly not only for transplantations, but also in the field of life science research. However, little information is available on the biological characteristics of CB units collected in rural areas because no medical facilities are affiliated with CB banks. Little attention has been paid to the collection of CB units in rural areas compared to CB collected in metropolitan areas. CB is a precious source for life science research due to the recent low birth rate in Japan. Therefore, to efficiently utilize CB units, the purpose of the present study was to investigate the optimum obstetric factors associated with a higher yield of mononuclear/CD34+ cells per CB unit. Methods:, CB units were collected at a single hospital (Hirosaki National Hospital). A total of 126 CB units from 105 vaginal deliveries and 21 cesarean section deliveries were available for cell separation within 24 h. Mononuclear low-density (LD) cells were separated using Ficoll-Paque and then processed for CD34+ cell enrichment using magnetic cell sorting. Associations between the maternal/neonatal factors and the yield of LD/CD34+ cells were analyzed. Results:, Despite the larger net weight of CB collected from cesarean section deliveries, the total number of LD cells collected from vaginal deliveries was significantly higher than that collected from cesarean section deliveries. The total number of LD cells per CB unit from primigravidae was significantly higher compared with that collected from from multigravidae. Conclusion:, CB units from vaginal deliveries of primigravidae may be more favorable because they contain a higher yield of mononuclear cells. [source] Liquid chromatography combined with mass spectrometry for 13C isotopic analysis in life science researchMASS SPECTROMETRY REVIEWS, Issue 6 2007Jean-Philippe Godin Abstract Among the different disciplines covered by mass spectrometry, measurement of 13C/12C isotopic ratio crosses a large section of disciplines from a tool revealing the origin of compounds to more recent approaches such as metabolomics and proteomics. Isotope ratio mass spectrometry (IRMS) and molecular mass spectrometry (MS) are the two most mature techniques for 13C isotopic analysis of compounds, respectively, for high and low-isotopic precision. For the sample introduction, the coupling of gas chromatography (GC) to either IRMS or MS is state of the art technique for targeted isotopic analysis of volatile analytes. However, liquid chromatography (LC) also needs to be considered as a tool for the sample introduction into IRMS or MS for 13C isotopic analyses of non-volatile analytes at natural abundance as well as for 13C-labeled compounds. This review presents the past and the current processes used to perform 13C isotopic analysis in combination with LC. It gives particular attention to the combination of LC with IRMS which started in the 1990's with the moving wire transport, then subsequently moved to the chemical reaction interface (CRI) and was made commercially available in 2004 with the wet chemical oxidation interface (LC-IRMS). The LC-IRMS method development is also discussed in this review, including the possible approaches for increasing selectivity and efficiency, for example, using a 100% aqueous mobile phase for the LC separation. In addition, applications for measuring 13C isotopic enrichments using atmospheric pressure LC-MS instruments with a quadrupole, a time-of-flight, and an ion trap analyzer are also discussed as well as a LC-ICPMS using a prototype instrument with two quadrupoles. © 2007 Wiley Periodicals, Inc., Mass Spec Rev 26:751,774, 2007 [source] | ||||||||||