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Fixation and Tissue Pretreatment
Published in Lars-Inge Larsson, Immunocytochemistry: Theory and Practice, 2020
Precipitating fixatives include ethanol, methanol, acetone. In the early days of immunocytochemistry, precipitating fixatives (e.g., cold acetone) were the agents of choice. Thus, they precipitated large protein molecules, and the protein “denaturation” was largely reversible. In a few applications, such precipitating fixatives have survived even up to the present day (cf. Reference 16 regarding fixations for IgG, IgA, and secretory component). One of the best methods for some antigens may still be the Saint-Marie procedure (details in Appendix).108 However, the precipitating fixatives are useless for EM studies, may produce considerable tissue shrinkage, and will actually extract most antigens. Moreover, as was discussed in the introduction, studies advocating specific fixation procedures for certain antigens usually fail to recognize that different antibodies detect different epitopes on proteins and should preferably incorporate studies of multiple distinct antibodies (perhaps raised to fixed antigens). This is the approach that is needed if immunoelectron microscopical studies are planned. In conclusion, precipitating fixatives may be useful for certain specific purposes, but if the studies have to incorporate electron microscopy, retrospective pathological material, or extractable antigens, or is otherwise bound by special requirements, precipitating fixatives are not a first-hand choice.
Transport of Radiolabeled Enzymes
Published in Lelio G. Colombetti, Biological Transport of Radiotracers, 2020
The most convenient procedure for protein/enzyme tritiation is the exchange of a hydrogen-3 ion supplied by tritiated water that is diluted in an organic solvent in the presence of a catalyst. The risk of protein denaturation seems very small. Evans et al.,11 Wilzbach,12 Means,13 and Bailey and Knowles14 described labeling procedures. Endert15 suggested the use of HPLC techniques for the separation of radiochemical impurities.
The Plant Kingdom
Published in Spyridon E. Kintzios, Maria G. Barberaki, Evangelia A. Flampouri, Plants That Fight Cancer, 2019
Peptides and proteins can be isolated from plant tissues by aqueous extraction or in less polar solvents (depending on the water solubility of a particular protein). Fractionation of the proteins can frequently be achieved by controlling the ionic strength of the medium through the use of salts. However, one must always take precautions against protein denaturation.
Green synthesis of ZnO-NPs using endophytic fungal extract of Xylaria arbuscula from Blumea axillaris and its biological applications
Published in Artificial Cells, Nanomedicine, and Biotechnology, 2023
Lavanya Nehru, Gayathri Devi Kandasamy, Vanaraj Sekar, Mohammed Ali Alshehri, Chellasamy Panneerselvam, Abdulrahman Alasmari, Preethi Kathirvel
Protein denaturation is the primary cause of inflammation, and the potential of the nanoparticle’s protein denaturation was investigated as a part of an inquiry into the mechanism of anti-inflammatory action [55]. Protein denaturation is a detrimental process in which a functional protein loses its biological function as a result of structural modifications spurred on by external stimuli such as chemicals, heat, etc. [56]. Anti-inflammatory activity is one of the intriguing studies that attempt to examine the protective ability of NPs rather than their destructive aspect [55]. Therefore, it is necessary to investigate the anti-inflammatory potential of the biosynthesized nanoparticles at the onset of their application as a therapeutic agent. The maximum inhibition of protein denaturation obtained employing the ZnONPs was found to be 96.77 ± 0.23% at 500 µg/mL concentration which was extremely close to the obtained value from the standard drug diclofenac sodium 98.45 ± 0.66% at maximum concentration, as shown in Table 5. Similarly, biogenic ZnONPs synthesised using L. edodes were found to inhibit protein denaturation in a dose-dependent manner with a maximum inhibition % of about 86.45 ± 0.60 in a similar trend of inhibition exhibited by diclofenac [57].
Thermophysical and mechanical properties of biological tissues as a function of temperature: a systematic literature review
Published in International Journal of Hyperthermia, 2022
Leonardo Bianchi, Fabiana Cavarzan, Lucia Ciampitti, Matteo Cremonesi, Francesca Grilli, Paola Saccomandi
Concerning the measurement of specific heat, it is important to point out that not all the heat supplied to biological tissue results in an increase in temperature since part of it is involved in endothermic reactions of denaturation of proteins present in the tissue. In studies using DSC to measure the specific heat, it is possible to observe that the trends present a maximum peak at protein denaturation temperatures (around 60 °C). In fact, due to the endothermic reactions of protein denaturation, the biological tissue requires a greater amount of heat to increase its temperature by 1 °C, i.e., it is characterized by a higher specific heat. For this reason, Choi et al. [156] decided to define the specific heat measured by DSC as ‘apparent specific heat’ in their discussion. In this regard, Watanabe et al. [157], in addition to DSC, used MDSC, since the latter allowed to eliminate the effect of endothermic reactions on specific heat measurements.
LncRNA miR143HG inhibits the proliferation of glioblastoma cells by sponging miR-504
Published in International Journal of Neuroscience, 2022
Peng Wang, Wenjuan Bao, Xiaopeng Liu, Wang Xi
Total proteins in 2 × 105 U-373 MG cells (collected at 24 h post-transfection) were extracted using RIPA solution (Sangon Biotech) and were quantified using BCA assay (Sangon Biotech). Protein denaturation was performed by incubating protein samples with boiling water for 5 min. Following electrophoresis performed using 12% SDS-PAGE gel proteins were transferred to PVDF membranes. After blocking performed in 5% non-fat milk (PBS), membranes were first incubated with anti-p53 (1: 1200, ab131442, Abcam) or anti-GAPDH (1: 1200, ab37168, Abcam) rabbit primary antibodies. After that, incubation with HRP (IgG) (1:1200; ab6721; Abcam) goat secondary antibody was performed. ECL™ Blocking Agent (Sigma-Aldrich) was used for signal production and Image J v1.48 software was used for data anlysis.