39 research outputs found
sj-docx-1-spp-10.1177_19485506241237288 – Supplemental material for Sexual (Double) Standards Revisited: Similarities and Differences in the Societal Evaluation of Male and Female Sexuality
No full textSupplemental material, sj-docx-1-spp-10.1177_19485506241237288 for Sexual (Double) Standards Revisited: Similarities and Differences in the Societal Evaluation of Male and Female Sexuality by Marcel Weber and Malte Friese in Social Psychological and Personality Science</p
Iodine Intake Increases IP-10 Expression in the Serum and Thyroids of Rats with Experimental Autoimmune Thyroiditis
No full textHere, we sought to establish an experimental autoimmune thyroiditis rat model induced by bovine thyroglobulin (bTg) injection and to investigate pathological changes and variations in serum interferon-γ-inducible protein of 10 kDa (IP-10) in thyroid tissue following iodine treatment. Four-week-old female Lewis rats (n=135) were randomly divided into normal (NC), thyroglobulin (TG), HI, HI+TG, HII, and HII+TG groups; rats in the NC and TG groups drank only distilled water (iodine concentration: 10 μg/L), rats in the HI and HI+TG groups were given water containing 25.7 mg/L iodine, and rats in the HII and HII+TG groups were given water containing 423.3 mg/L iodine. Rats in the TG, HI+TG, and HII+TG groups were immunized with 0.1 mL bTg (8 mg/mL) in incomplete Freund’s adjuvant once every 2 weeks for 6 weeks. Compared with the NC group, the TG, HI+TG, and HII+TG groups exhibited higher iodine intake and increased thyroid weights with increasing iodine doses (P<0.05). The high iodine intake in the TG group was associated with increased CD4+ T cells and serum IP-10. Thus, high iodine consumption aggravated the inflammatory reaction in the thyroid and mild high iodine consumption increased serum IP-10 levels after induction with bTg
Hicri 3. asrın başlarında sünnete sarılmak: “saç-sakalını da boyardı!”
No full textRavilerin hadis ilmi açısından ehliyetlerini tespit etmeyi hedefleyen biyografik eserlerde, birtakım ravilerin saç-sakallarını boyayıp boyamadıklarına dair kayıtlara tesadüf edilir. Bu makale doğrudan cerḥ-taʿdīl ile irtibatı olmayan bu verilerin biyografi türü eserlere hangi dönemde ve hangi etkilerle girdiğini tespit etmeyi hedeflemektedir. Söz konusu kayıtların hicri 3. asrın başlarında artması, konunun devrin sosyal, siyasi ve ilmî tartışmaları çerçevesinde ele alınmasını gerektirmektedir. Konu bu açıdan incelendiğinde saç-sakal boyamaya dair kayıtların Miḥne hadisesi ve bu süreçte siyasi erkin baskısına maruz kalan Aḥmed b. Ḥanbel ile irtibatı dikkat çekmektedir. Anlaşıldığı kadarıyla o, ihya edilmek istenen bir sünnet olarak gördüğü saç-sakal boyama faaliyetini, siyasi erki hedef alan bir pasif direniş tarzı olarak konumlandırmıştı. Ancak erken dönem boyama faaliyetleri ile Aḥmed b. Ḥanbel dönemi ve sonrasındaki faaliyetlerin her biri, tarz, amaç ve muhataplar bakımından farklılık arz etmektedir. Sonuç olarak makale hem ricāl metinlerindeki dönemsel etkileri tartışmakta hem de boyama faaliyetine yüklenen anlamın değişim serüvenini rivayet metinleri üzerinden takip etmektedir
Design and cloning strategy of the PHILODiamond antibody library.
No full text<p>(A, B) Three-dimensional structure of a scFv antibody fragment, with randomized amino acids highlighted in circles. In the DP47 heavy chain fragment (in red) position 95–100 were randomly mutated and the length of the CDR varies from 4 to 7 amino acids. A point mutation at position 52, short before the CDR2, was introduced converting a Ser to an Asn, as marked with a star. The antibody in (A) shows the DPK22 light chain fragment (in blue), in which the Pro95 was kept constant and a Gly residue was allowed to be located at position 92 or 93. The antibody in (B) contains a light chain based on the DPL16 germline segment. The CDR3 of light chain contains at least one Pro residue, either at position 91, 92, 93, 94 or 95. (C) Cloning strategy for the construction of different sub-libraries, which were eventually pooled to yield the PHILODiamond library. Primers are listed in <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0100000#pone.0100000.s002" target="_blank">Figure S2</a>. Two different cloning strategies were used. In the <i>not-</i>strategy, two DNA fragments coding for the heavy or light chain respectively were assembled and amplified using a primer containing the <i>Not</i>I-restriction site. In the <i>abc-</i>strategy, an additional DNA segment, which contained the <i>Not</i>I-restriction site, was assembled together with the randomized light and heavy chain fragments. (D) All DNA fragments were amplified, double digested and ligated into the pHEN1 phagemid vector. All numbers in the antibody sequences are according to Tomlinson et al <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0100000#pone.0100000-Tomlinson3" target="_blank">[43]</a>. The three-dimensional structures were modelled from the Protein Data Bank files 1IGM (DPK22) and 8FAB (DPL16).</p
Analysis of the length of the randomized residues in CDR3 of the heavy chain from well characterized clones, isolated from the PHILODiamond and the ETH2Gold libraries against several antigens (selections performed in parallel).
No full text<p>In the ETH2Gold library, the CDR3 loops of the heavy chain contained between 4 and 6 randomized consecutive amino acids, while in PHILODiamond between 4 and 7 amino acids were randomized. The PHILODiamond library exhibited a trend towards the isolation of scFv clones with longer CDR3 loops.</p
Biacore profiles of representative scFv fragments.
No full text<p>The Biacore experiments were performed using monomeric preparations of scFv fragments specific to 12 different antigens (listed in the Figure) after bacterial expression, protein A purification and Superdex-75 gel filtration chromatography. The concentrations of the scFv were between 150 nM and 450 nM. RU: resonance units.</p
Quality controls on the antibody library.
No full text<p>(A) Representative dot-blot analysis of 94 supernatants of individual unselected library clones. The soluble scFv fragments in the bacterial supernatants were detected using an anti-myc-tag antibody (9E10) and a secondary antibody coupled with HRP. As positive control, a purified scFv fragment with a myc-tag was loaded (green circle). As a negative control, 2xYT medium was used (red circle). (B) A representative agarose gel of the PCR colony screening of unselected clones from the library, used primers capable of amplifying the scFv insert. As a negative control, non-transfected bacteria (left red arrow) and bacteria containing pHEN1 vector with a longer insert (right red arrow) were used. As a positive control, a phagemid vector with a scFv insert was used (green arrow). All six dot-blots and PCR-screening gels related to the library construction process are shown in <b><a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0100000#pone.0100000.s002" target="_blank">Figure S2</a></b>.</p
Characterization of the G5 antibody, specific to the alternatively spliced BCD domains of tenascin-C.
No full text<p>(A) Schematic representation of the scFv and SIP antibody format. (B) Biacore characterization of the monomeric fraction of scFv (G5) produced at different concentrations on a CM5 Biacore microsensor chip, coated either with murine (left) or human recombinant BCD domains of tenascin-C (right). (C) SDS-PAGE of the G5 antibody in SIP format in reducing (R) and nonreducing (N) conditions, as well as gel-filtration profile on a S200 10/300 column. (D) Biacore profiles of the G5 antibody in SIP format, against murine and human recombinant BCD domains of tenascin-C.</p
Immunofluorescence analysis of tumor sections.
No full text<p>The staining properties of the G5 antibody were studied by immunofluorescence on frozen sections, derived from tumors grafted subcutaneously in mice. The staining results with G5 were compared to the ones of F16 (a clinical-state human antibody specific to the human, but not murine, alternatively spliced A1 domain of tenascin-C), F8 (a clinical-state human antibody specific to the alternatively spliced EDA domain of fibronectin, which recognizes the cognate antigen in mouse and man) and as a negative control KSF (specific to hen-egg lysozyme). All antibodies were tested in SIP format.</p
