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Introduction: Inflammation is body's immune response to harmful stimulus. Commonly used conventional antiinflammatory agents are Non-Steroidal Anti-inflammatory Drugs (NSAIDs). But on prolonged long-term use, it causes serious adverse events. So, the search towards natural agents which have anti-inflammatory property are increasing nowadays. Sinapis arvensis is an annual flowering plant which has proven multipurpose medicinal phytoconstituents. Aim: To evaluate in-vitro anti-inflammatory effects of flower extracts of Sinapis arvensis with diclofenac as standard. Materials and Methods: This in-vitro study assessed the laboratory based anti-inflammatory activity, performed using Bovine Serum Albumin (BSA) assay in December 2021 at Sree Balaji Medical College and Hospital, Chennai, Tamil Nadu, India. BSA at pH of 6.8 generated denatured proteins. The anti-inflammatory activity of the sample (flower extracts of Sinapis arvensis) and standard (Diclofenac) was assessed by adding to BSA and percentage of inhibition of denaturation were calculated using the formula based on the absorbance measured. Descriptive statistics was used for analysis of collected data. Results: The concentration-dependent inhibition of protein denaturation was observed for both Sinapis arvensis and Diclofenac. At 100 µg concentration, percentage of inhibition reached up to 81.8% and 100% for Sinapis arvensis and Diclofenac, respectively. Conclusion: The present study showed that flower extracts of Sinapis arvensis exhibited concentration dependent antiinflammatory property invitro which proves to be nearly equivalent with that of the standard Diclofenac. [ABSTRACT FROM AUTHOR]

Introduction: Ashwagandha (Withania somnifera) is an important medicinal plant in Indian traditional system of medicine and traditionally has been used for several medicinal purposes in India. The present study was conducted to evaluate the anti-inflammatory effect of hydroalcoholic extract of ashwagandha against denaturation of protein in vitro. Methods: The test extract at different concentrations was incubated with egg albumin in controlled experimental conditions and subjected to determination of absorbance and viscosity to assess the anti-inflammatory property. Diclofenac sodium was used as the reference drug. Results: The present results exhibited a concentration dependent inhibition of protein (albumin) denaturation by the ashwagandha extract. The effect of diclofenac sodium was found to be less when compared with the test extract. Conclusion: Form the present findings it can be concluded that ashwagandha possessed marked anti-inflammatory effect against denaturation of protein in vitro. The effect was plausibly due to the alkaloid and withanolide contents of ashwagandha. [ABSTRACT FROM AUTHOR]

The ESAT-6 family proteins of Mycobacterium tuberculosis are regarded as the key mediators in mycobacterial virulence and are largely considered as antigens that can improve TB vaccines and diagnostics. We have characterized Rv3444c and Rv3445c proteins of the ESX-4 system of ESAT-6 family of M. tuberculosis H37Rv, and have experimentally established that these two proteins interact to form a heterodimeric complex. Complex formation resulted in induction of α-helical conformation and stability against chemical denaturation. To evaluate the immunogenic potential, we have immunized mice with Rv3444c or Rv3445c along with Freund's incomplete adjuvant (FIA). Immunization with Rv3444c-FIA or Rv3445c-FIA resulted in long term humoral responses. Re-stimulation of splenocytes from immunized mice resulted in significant lymphocyte proliferation with induction of TNF-α and IL-6. Further, the humoral responses to Rv3444c and Rv3445c antigens in Indian patients with active pulmonary TB (n = 44), and healthy individuals (n = 20), were investigated. Compared to healthy individuals, high levels of IgG against Rv3444c and Rv3445c were observed in TB patient's sera, indicating that these proteins are actively produced during the active phase of TB. Cellular immune responses to these proteins in active pulmonary TB patients (n = 5) were also investigated using peripheral blood mononuclear cells (PBMCs). Both the proteins induce significant lymphocyte proliferation and up-regulate the induction of TNF-α and IL-6 in TB patients., (Copyright © 2018 Elsevier Ltd. All rights reserved.)

Background: Heat treatment is the most common method for reducing pathogen load, but it remains controversial in reducing the incidence of hyperimmune reactions. The aim of this study was to compare the allergenicity of caseins (CSN) and whey proteins (WP) of thermally processed cow and buffalo milk in a mouse model. Swiss albino mice were sensitised by intraperitoneal injections (administered in three doses at weekly intervals) of CSN or WP from cow or buffalo milk for the evaluation of humoral response and splenocyte stimulation index., Results: After 3 weeks of intraperitoneal stimulation of mice with milk proteins, the sterilised milk protein group displayed significantly lowered (P ≤ 0.05) serum IgG and IgE levels, while considerably increased cow milk protein-specific responses (IgE) were shown by proteins of pasteurised milk compared with those of raw milk. The stimulation index of splenocytes induced by CSN or WP of boiled and sterilised milk was also lower (P ≤ 0.05) than that of raw milk of both cow and buffalo., Conclusion: The experiment showed that boiling and sterilisation of cow and buffalo milk clearly affect the allergenicity by decreasing the humoral and cell-mediated responses in mice. All results indicated that CSN and WP of sterilised milk are less allergenic than those of raw milk in mice., (© 2013 Society of Chemical Industry.)

The fibrinolytic components of venom have been evaluated for long in the enzymatic treatment of thrombosis. Russell's viper venom has fibrinolytic activity that is associated with hemorrhagic activity. Here it has been investigated whether the crude venom could be detoxified by thermal denaturation retaining fibrinolytic activity. The venom at 0.05 mg/ml in 20 mM K-phosphate, pH 7.5 when exposed to 100 °C for 5 min followed by cooling at 25 °C for 1 h led to its detoxification, while 80-85% of the fibrinolytic activity was recovered. Assessment of toxicity of the renatured venom in mice after injection at 5 fold excess of the lethal dose showed no lethality including hemorrhage, myotoxicity, cytotoxicity and liver toxicity. This simple method for preparation of fibrinolytic component for therapeutic use may be developed., (Copyright © 2011 Elsevier Ltd. All rights reserved.)

The electrophoretic variant of human LDH, Calcutta-1, occurs at phenotypic frequencies of 0-4% throughout India. The variant was examined by various electrophoretic techniques and by heat stability studies. The LD1 (B4) isoenzyme was purified from normal and variant bloods by affinity chromatography and ion-exchange chromatography. A minimum of five Calcutta-1 LD1 bands was demonstrated by isoelectric focusing. Electrophoresis of variant LD1 in high-molar urea-acrylamide denaturing gels resulted in two Calcutta-1 B subunit bands, while normal gels yielded only a single band. Homozygote Calcutta-1 LDH from red cells demonstrated a decreased heat stability, while heterozygote variant LDH showed a normal heat stability. This effect was confirmed when purified LD1's were compared. Evidence is presented suggesting a B-subunit variant showing thermolability in the homozygous form.