“
“Sericin is a protein present in

silk cocoons, which envelopes the fibers with sticky layers. Silk proteins ( Sericin and fibroin) are biodegradable and biocompatible. If the sericin is recovered, it can present significant SNX-5422 chemical structure and social benefits, as it is discarded in silk processing industry along with waste water. The influence of sericin, as a binding agent, on bulk, compressional and tabletting characteristics of propranalol Hydrochloride tablet formulation was studied in comparison with the effect of standard binder, starch. Method of sericin extraction was developed and optimized and the yield was 12.75%. Granules, containing Propranalol HCl, were prepared and evaluated for crushing strength, friability and flowability. Granules showed comparable physical characteristics concerning flow properties and crushing strength. Tablets were prepared using sericin and starch Z-DEVD-FMK as a binder separately and compared for weight variation, hardness, friability, and disintegration and in-vitro dissolution. Sericin yield was 12.75%. Tablets made from sericin had the highest crushing strength and lowest tendency to laminate. All the formulated tablets had friability values less than 1% at the concentration used in the study. Granules exhibited angle of repose in the range

of 29(0)-31(0) and crushing strength ranged between 400-600 gms. Sericin did not influence the dissolution of drug by its presence in the dosage form. Two-way ANOVA test showed no significant differences for tablet parameters. Sericin as a binder was comparable to potato starch. The characterization of the formulation suggests that sericin can be developed in to a commercial binding agent for tablets.”
“Normal atrial conduction requires similar abundances and homogeneous/overlapping distributions of two connexins (Cx40 and Cx43). The remodeling of myocyte connections and altered electrical conduction associated with atrial fibrillation (AF) likely involves perturbations

of these connexins. Rocilinostat We conducted a comprehensive series of experiments to examine the abundances and distributions of Cx40 and Cx43 in the atria of AF patients. Atrial appendage tissues were obtained from patients with lone AF (paroxysmal or chronic) or normal controls. Connexins were localized by double label immunofluorescence confocal microscopy, and their overlap was quantified. Connexin proteins and mRNAs were quantified by immunoblotting and gRT-PCR. PCR amplified genomic DNA was sequenced to screen for connexin gene mutations or polymorphisms. Immunoblotting showed reductions of Cx40 protein (to 77% or 49% of control values in samples from patients with paroxysmal and chronic AF, respectively), but no significant changes of Cx43 protein levels in samples from AF patients. The extent of Cx43 immunostaining and its distribution relative to N-cadherin were preserved in the AF patient samples.