Beat to Beat: Implementing a Tailored Literature Review e-Newsletter for a Multidisciplinary Subspecialty Group

Objective: To increase availability and exposure to recent, relevant, reliable literature from a range of sources, for a multidisciplinary cardiac center, by creating an e-newsletter summarizing articles of interest.https://jdc.jefferson.edu/patientsafetyposters/1043/thumbnail.jp

Evaluation of a continuous chromatography process through process modeling and resin characterization

Increased product yield at reduced cost and time has been the driving force of any manufacturing process. However, inevitable increase in future demand for biopharmaceutical drugs, along with intensified competition and stringent regulatory laws have exhibited an imperative need for established platform processes. In this regard, the implementation of continuous processing, in whole or in components, has demonstrated to increase the manufacturing productivity with key impact on speed, cost and facility implications. While, upstream operations have confirmed increased productivity by implementation of continuous processing components, such as perfusion culture, similar adaptation for downstream processes has been limited. We have evaluated a continuous process for separation of a mAb in a closed environment by employing a combined approach of process modelling for continuous chromatography column and characterization of the Protein A resin. The process model utilized several semi-empirical parameters namely Peclet number and effective diffusivity from previous batch processes for continuous separation mAbs, which were appraised for process efficiency. The resin characteristics were assessed for the impact of pH, temperature, pressure and shelf life using the Scanning Electron Microscope (SEM). The results and associated outcome confirmed that this model can be employed with significant impact on the process time. The approach elucidates the conditions required to perform the continuous unit operation for mAb capture step, with indications of alleviating the bottleneck posed by conventional batch processes. Overall, the outcomes of the evaluated approach supports the shift away from conventional fed batch processes to continuous processing for improved biomanufacturing

Concept of Fatty liver and its management in Ayurveda

Fatty liver disease is a most common liver disease affecting a wide range of population worldwide. It is caused due to excessive fat accumulation in liver cells resulting in inflammation in liver. There are various symptoms such as confusion, fatigue, weakness etc. Over-eating is the major lifestyle factor causing fatty liver disease. Alcoholic intake results in alcoholic fatty liver disease Ajirna (indigestion), Sthaulya (obesity) and Prameha (diabetes mellitus) which occurs due to the vitiation of Annavaha, Rasavaha and Medovaha Srotas acts as Nidanarthakara Rogas (diseases which cause another diseases) which may result in the manifestation of non-alcoholic fatty liver. According to Ayurvedic texts, Panchkarma (Virechana) and herbs like Bhumiamalaki and Guduchi etc. acts a hepatoprotective and improves the functioning of liver

Interaction of thiocyanate with horseradish peroxidase. <SUP>1</SUP>H and <SUP>15</SUP>N nuclear magnetic resonance studies

Interaction of thiocyanate with horseradish peroxidase (HRP) was investigated by relaxation rate measurements (at 50.68 MHz) of the 15N resonance of thiocyanate nitrogen and by following the hyperfine shifted ring methyl proton resonances (at 500 MHz) of the heme group of SCN-.HRP solutions. At pH 4.0, the apparent dissociation constant (KD) for thiocyanate binding to HRP was deduced to be 158 mM from the relaxation rate measurements. Chemical shift changes of 1- and 8-ring methyl proton resonances in the presence of various amounts of thiocyanate at pH 4.0 yielded KD values of 166 and 136 mM, respectively. From the pH dependence of KD and the 15N resonance line width, it was observed that thiocyanate binds to HRP only under acidic conditions (pH &lt; 6). The binding was found to be facilitated by protonation of an acid group on the enzyme with pKa 4.0. The pH dependence of the 15N line width as well as the apparent dissociation constant were quantitatively analyzed on the basis of a reaction scheme in which thiocyanate in deprotonated ionic form binds to the enzyme in protonated acidic form. The KD for thiocyanate binding to HRP was also evaluated in the presence of an excess of exogenous substrates such as resorcinol, cyanide, and iodide ions. It was found that the presence of cyanide (which binds to heme iron at the sixth coordination position) and resorcinol did not have any effect on the binding of thiocyanate, indicating that the binding site of the thiocyanate ion is located away from the ferric center as well as from the aromatic donor binding site. The KD in the presence of iodide, however, showed that iodide competes with thiocyanate for binding at the same site. The distance of the bound thiocyanate ion from the ferric center was deduced from the 15N relaxation time measurements and was found to be a 6.8 &#197;. From the distance as well as the change in the chemical shifts and line width of 1- and 8-methyl proton resonances, it is suggested that the binding site of thiocyanate may be located near heme, placed symmetrically with respect to 1- and 8-methyl groups of the heme of HRP. Similarity in the modes of binding of iodide and thiocyanate suggests that the oxidation of thiocyanate ion by H2O2 may also proceed via the two-electron transfer pathway under acidic conditions, as is the case for iodide