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Direct Oral Anticoagulants: New Options
Published in Peter Grunwald, Pharmaceutical Biocatalysis, 2020
To avoid excessive coagulation, the process is physiologically controlled either by enzyme inhibition or by modulation of the activity of the cofactors (Dahlback, 2000). Tissue factor pathway inhibitor (TFPI) inhibits the initiation of coagulation by forming a complex with FXa, which then binds to TF/FVIIa. The serpin (i.e., serine protease inhibitor) antithrombin (AT) inactivates most of the serine proteases generated during activation of coagulation. The inhibitory potency of this rather slow-reacting inhibitor is enhanced by binding to endothelial heparan sulfate (Alban, 2008a). Similarly, the thrombin inhibitor heparin cofactor II (HCII) is stimulated by binding to glycosaminoglycans.
Ozone-induced acute phase response in lung versus liver: the role of adrenal-derived stress hormones
Published in Journal of Toxicology and Environmental Health, Part A, 2021
Devin I. Alewel, Andres R. Henriquez, Catherine H. Colonna, Samantha J. Snow, Mette C. Schladweiler, Colette N. Miller, Urmila P. Kodavanti
For Study 1, total RNA samples were diluted to 10 ng/μl. Using 50 ng RNA, one-step qPCR was performed using Superscript III kit (Invitrogen, Waltham, MA) and DNA amplification was assessed using an ABI Prism 7900 HT sequence detection system (Applied Biosystems, Foster City, CA). Primers purchased from Applied Biosystems (Foster City, CA) containing a 6-carboxy-fluorescein (FAM dye) 5ʹ label was employed for the following genes: β-actin (Actb, Rn00667869_m1), α2-macroglobulin (A2m, Rn00560589_m1), orosomucoid-1 (Orm1, Rn00583913_m1), serpin peptidase inhibitor, clade A, member 1 (Serpina1, Rn00574670_m1), C-reactive protein (Crp, Rn00567307_g1), haptoglobin (Hp, Rn00561393_m1), ceruloplasmin (Cp, Rn00561049_m1), and hepcidin (Hamp, Rn00584987_m1). Using Actb as an endogenous control, data were analyzed via ABI software, version 2.2. Relative expression for Day 1 and Day 2 rats were calculated separately in relation to fold change from respective air-exposed rats of each day for a given tissue using the 2−ΔΔCT method.
Ovalbumin at oil–water interfaces: Adsorption and emulsification
Published in Journal of Dispersion Science and Technology, 2018
Bhawna Panjwani, Sharad Gupta, Prachi Thareja
OVA is a globular protein obtained from the chicken egg white, belonging to the serpin superfamily with 385 amino acids. It was supplied by Sigma Aldrich and was used as received (MW 44.3 kDa). CO, SBO, and OO were obtained from the local market and were used without further purification. All the studies were carried out using ultrapure water from a Millipore system (18.2 MΩ.cm at 25°C). The composition and properties of the oils are summarized in Table 1.