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Host-Parasite Interactions With Macrophages In Culture
Published in Hans H. Gadebusch, Phagocytes and Cellular Immunity, 2020
Lee S. F. Soderberg, Morris Solotorovsky
The macrophage presentation model does not at first inspection account for the ability of 5 x 105 M 2-mercaptoethanol to supplant the adherent cell requirement in certain antibody-forming systems.12 This model also cannot account for the ability of cell-free supernatant fluids to replace macrophage function in the development of in vitro antibody responses by purified lymphocytes.13 An alternative model attributes to macrophages a function of promoting lymphocyte viability via a soluble substance or factor since nonresponsiveness in the above illustrations is accompanied by loss of lymphocyte viability. The function of 2-mercaptoethanol in replacing macrophages has not been well characterized but recent evidence suggests that it interacts with fetal calf serum to become nonspecifically mitogenic for B lymphocytes.14 The 2-mercaptoethanol enhancement appears to be purely an in vitro phenomenon. Thus the antigen presentation model remains an attractive model of macrophage function while the 2-mercaptoethanol experiments show that macrophage activity is nonspecific.
Renal Effects
Published in Lars Friberg, Tord Kjellström, Carl-Gustaf Elinder, Gunnar F. Nordberg, Cadmium and Health: A Toxicological and Epidemiological Appraisal, 2019
Acute renal effects following injections of cadmium chloride bound to mercaptoethanol have been reported by Gieske and Foulkes.78 They found a decreased PAH clearance and a decreased tubular reabsorption of all amino acids, indicating a tubular damage 3 days after a single intravenous (i.v.) injection of CdCl2-mercaptoethanol mixture (1.1 mg Cd).
Incapacitating Agents and Technologies: A Review *
Published in Brian J. Lukey, James A. Romano, Salem Harry, Chemical Warfare Agents, 2019
2-Mercaptoethanol is also known as thioglycol. It is a colorless combustible liquid having a very unpleasant disagreeable odor and a vapor pressure of 1 mm Hg (208°C) (Lewis, 1993). A workplace environmental exposure level (WEEL) of 0.2 ppm as a TWA8 has been proposed by the American Industrial Hygiene Association. Acute lethal toxicity data are as follows: p.o. LD50 (rat) 131 mg kg−1; percutaneous LD50 (rabbit) 251 mg kg−1, (guinea pig) 300 mg kg−1; 4 h LC50 (rat) 2 mg L−1. It is a skin and eye irritant (Mallinckrodt Baker, 2004; Chevron Phillips, 2005).
Current trends in the use of human serum albumin for drug delivery in cancer
Published in Expert Opinion on Drug Delivery, 2022
Milan Paul, Asif Mohd Itoo, Balaram Ghosh, Swati Biswas
This method involves hydrophobization of albumin by conjugating hydrophobic moiety to the albumin (Figure 2C). The primary site for conjugation could be the amine group that conjugates acidic moiety via acid-amine coupling reaction using zero-order crosslinking agents, usually the combination of ethyl(dimethyl aminopropyl)carbodiimide and N-hydroxysuccinimide. Breaking of disulfide bonds using β-mercaptoethanol increases hydrophobicity and allows thiol-mediated conjugation. In our effort to form a core-shell structure, albumin was conjugated to a lipid, dioleoyl phosphatidylethanolamine (DOPE) [35]. The conjugate self-assembled to form spherical NPs (~210 nm) with high encapsulation efficiency (79%) and loading (21%) of a hydrophobic anticancer agent, curcumin. Another albumin-based core-shell NPs were prepared by conjugating vitamin E to albumin. The NPs-loaded paclitaxel efficiently with high drug entrapment (95.7%) and loading efficiency (12.5%) and displayed particle size of ~100 nm [40].
Evaluation of similar quality attribute characteristics in SB5 and reference product of adalimumab
Published in mAbs, 2019
Nayoung Lee, JongAh Joanne Lee, Hahymn Yang, Serim Baek, Soohwan Kim, Sooshin Kim, Tongkeun Lee, Dami Song, Gwangmin Park
Reducing and non-reducing CE-SDS analyses were conducted with a high-performance capillary electrophoresis system (PA 800 plus Pharmaceutical Analysis System; Beckman coulter). For the reducing condition, sample (200 µg) was mixed with 2 µL of a 10 kDa internal standard, 91 µL of SDS-MW sample buffer (Beckman coulter, A10663), and 5 µL of 2-mercaptoethanol and then boiled at 70°C for 5 minutes. For the non-reducing condition, 2-mercaptoethanol was replaced with iodoacetamide. The sample was electrokinetically introduced onto a capillary (Beckman Coulter, bare fused-silica capillary, 50 µm/30.2 cm) by applying voltage at −5 kV for 20 seconds and was separated in the capillary cartridge. Electrophoresis was performed at a constant voltage with an applied field strength of −497 volts and monitored by UV detection (λ = 220 nm) through the capillary window and aperture (Beckman Coulter, 144712, 100 × 200 µm). Data were acquired and processed by 32 Karat software with integration capabilities.
Thermostability enhancement of the α-carbonic anhydrase from Sulfurihydrogenibium yellowstonense by using the anchoring-and-self-labelling-protein-tag system (ASLtag)
Published in Journal of Enzyme Inhibition and Medicinal Chemistry, 2019
Sonia Del Prete, Rosa Merlo, Anna Valenti, Rosanna Mattossovich, Mosè Rossi, Vincenzo Carginale, Claudiu T. Supuran, Giuseppe Perugino, Clemente Capasso
CA activity assay was a modification of the procedure described by Capasso et al.59. Briefly, the assay was performed at 0 °C using CO2 as substrate and following the pH variation due to the catalysed conversion of CO2 to bicarbonate. Bromothymol blue was used as the indicator of pH variation. The production of hydrogen ions during the CO2 hydration reaction lowers the pH of the solution until the colour transition point of the dye is reached. The time required for the colour change is inversely related to the quantity of CA present in the sample. Wilbur-Anderson units (WAU) were calculated according to the following definition: one WAU of activity is defined as (T0−T)/T, where T0 (uncatalysed reaction) and T (catalysed reaction) are recorded as the time (in seconds) required for the pH to drop from 8.3 to the transition point of the dye in a control buffer and in the presence of enzyme, respectively. Assay of the membrane-bound enzyme (H5-SspCA or SspCA) was carried out using an amount of whole cells or outer membranes ranging from 1.0 to 5.0 mg. Sodium dodecyl sulphate (SDS)-polyacrylamide gel electrophoresis (PAGE) was performed as described by Laemmli using 12% gels.60 Samples were dissolved in buffer with 5% β-mercaptoethanol. The gel was stained with Coomassie blue and protein concentration was determined by Bio-Rad assay kit (Bio-Rad, Hercules, CA).