Solvers for the cardiac bidomain equations

The bidomain equations are widely used for the simulation of electrical activity in cardiac tissue. They are especially important for accurately modeling extracellular stimulation, as evidenced by their prediction of virtual electrode polarization before experimental verification. However, solution of the equations is computationally expensive due to the fine spatial and temporal discretization needed. This limits the size and duration of the problem which can be modeled. Regardless of the specific form into which they are cast, the computational bottleneck becomes the repeated solution of a large, linear system. The purpose of this review is to give an overview of the equations and the methods by which they have been solved. Of particular note are recent developments in multigrid methods, which have proven to be the most efficient.     

Polygalacturonase Inhibiting Proteins (PGIPs) of Plants

Polygalacturonase inhibiting proteins (PGIPs) are widely distributed in plants and appear to play an important role in protection of plants from fungal infection and also in maturation and ripening of fruits. They are leucine rich thermostable glycoproteins of about 40 kD and exhibit differential inhibition of polygalacturonases from different sources. A lot of attention is now being paid to these proteins with respect to their physicochemical and biological properties and also to their genes. These proteins show a lot of sequence homology to several signal transduction molecules from diverse species and have been suggested to play a similar role in plants. These proteins are also potentially important from biotechnological perspective. This review focuses on the recent work carried on PGIPs and its implications.     

Rotifera from Burundi: the Lepadellidae (Rotifera: Monogononta)

We studied the distribution of Lepadellidae (Rotifera) in freshwater habitats in the floodplain of the River Rusizi in northwest Burundi. Twenty-three species belonging to ColurellaBory de St. Vincent, 1824 (3 species), Lepadella Bory de St. Vincent, 1826 (18 species) and Squatinella Bory de St. Vincent, 1826 (2 species) are recorded, 22 of them are new to Burundi. One of the taxa encountered probably represents an unnamed species. Lepadella arabicaSegers & Dumont, 1993 is recognised as junior subjective synonym of Lepadella eurysterna Myers, 1942 (syn. nov.). Most of the taxa recorded are cosmopolitan or tropicopolitan, two are restricted to the tropical regions of the Old World and Australia, and one, Squatinella lunata Segers, 1993 is an Ethiopian endemic.     

Thermocyclops dumonti sp. n. (Crustacea,Copepoda), from a Temporary Waterbody in China

Six species of the genus Thermocyclops have hitherto been known from Chinese freshwaters. A new species is here recorded from a sample collected from an eutrophic pool in central China. It is described and compared using classical morphology and mapping of its pore signature. Thermocyclops dumonti differs from T. kawamurai by absence of ornamentation on prominences of intercoxal plates of P₁‐P₃, by relative length of apical spines of Enp₃P₄ and caudal ramus. It differs from T. dybowskii by ornamentation of P₄ intercoxal plate, relative length of Enp₃P₄ and caudal ramus, by shape of Tmi. As in other species of Thermocyclops, the perforations are bilaterally symmetrical and, species‐specific patterns occur on the cephalosome, metasome, and urosome. Conserved patterns are found elsewhere on the rostrum, cephalosome, metasome, and furcal branches. Based on pore pattern, Thermocyclops dumonti is separated from two close relatives, T. schmeili and T. dybowskii.     

Drimarene brilliant blue--a better pre-stain in protein separation and visualization.

Prestaining of human serum proteins with a new reactive dye Drimarene Brilliant Blue (DBB), was standardized employing 940 separations and examining 30 variables. Under the critical condition, the serum and the soluble dye (0.1 g/100 ml in working Tris-glycine buffer, pH, 8.3), was mixed in equal proportion, conjugate warmed at 40 degrees C for 2 hr and a 30 microliter of the sample electrophoresed by disc electrophoresis. The method when compared with prestaining by Remazol Brilliant Blue (RBB) and postelectrophoretic staining by Amido Black (AB) in 50 normal sera, revealed that the discs stained with DBB were intense and well defined and appeared in 2 hr on a sparkingly clear gel. Quality of resolution was better than RBB and AB. Protein bands eluted from the DBB prestained gels retained their immunoreactivity. The dye-protein complex of albumin and transferrin produced high-titre monospecific antisera in rabbits.     

Effect of nitrogen supplementation on the longevity of antibiotic production by immobilized cells of Penicillium urticae

Summary Conidia of Penicillium urticae were immobilized in Kappa-Carrageenan beads (2–3 mm) by a previously described procedure to yield an in situ grown immobilized cell population which could be induced to produce the antibiotic and mycotoxin, patulin. When repeatedly transferred into a nitrogen-free production medium every 2 days, the patulin productivity of these cells gradually decreased to 50% within 14 days while the total cell protein remained constant. This decline was due to the gradual loss of the cells' catalytic capacity for converting glucose to 6-methylsalicylic acid (6-MSA), the first metabolite of the patulin pathway, as well as for converting 6-MSA to patulin. When these 14 day-old cells were incubated in a nutrient rich growth medium for 2 days their patulin producing activity increased from 50% to 130%. On the other hand the addition of a protein synthesis inhibitor, cycloheximide, to the N-free production medium drastically reduced the patulin producing activity of the immobilized cells; in particular, their capacity for converting 6-MSA to patulin. The cells' patulin producing activity was maintained at >100% for longer than 15 days when the cells were repeatedly transferred into a yeast extract supplemented production medium or when they were occasionally transferred into 10 or 20% strength growth medium. Repeated transfers to a 10% strength growth medium appeared to stabilize the cells' capacity for converting 6-MSA to patulin.     

Competitive binding assay using fluorescence resonance energy transfer for the identification of calmodulin antagonists

The ubiquitous calcium regulating protein calmodulin (CaM) has been utilized as a model drug target in the design of a competitive binding fluorescence resonance energy transfer assay for pharmacological screening. The protein was labeled by covalently attaching the thiol-reactive fluorophore, N-[2-(1-maleimidyl)ethyl]-7-(diethylamino)coumarin-3-carboxamide (MDCC) to an engineered C-terminal cysteine residue. Binding of the environmentally sensitive hydrophobic probe 2,6-anilinonaphthalene sulfonate (2,6-ANS) to CaM could be monitored by an increase in the fluorescence emission intensity of the 2,6-ANS. Evidence of fluorescence resonance energy transfer (FRET) from 2,6-ANS (acting as a donor) to MDCC (the acceptor in this system) was also observed; fluorescence emission representative of MDCC could be seen after samples were excited at a wavelength specific for 2,6-ANS. The FRET signal was monitored as a function of the concentration of calmodulin antagonists in solution. Calibration curves for both a selection of small molecules and a series of peptides based upon known CaM-binding domains were obtained using this system. The assay demonstrated dose-dependent antagonism by analytes known to hinder the biological activity of CaM. These data indicate that the presence of molecules known to bind CaM interfere with the ability of FRET to occur, thus leading to a concentration-dependent decrease of the ratio of acceptor:donor fluorescence emission. This assay can serve as a general model for the development of other protein binding assays intended to screen for molecules with preferred binding activity.