Effects of chronic low-frequency electrical stimulation of human knee extensor muscles exposed to static passive stretching

The study investigated the effects of chronic low-frequency electrical stimulation (CLFES) of the stretched knee extensor muscles versus CLFES without a resistance load. A total of 19 male volunteers were randomized into two groups with similar aerobic and force-velocity properties. In group 1, anterior thigh muscles (the knee extensors) of both legs were exposed to CLFES (15 Hz). In group 2, the CLFES of the knee extensors was combined with stretching. The stimulated subjects demonstrated a marked tendency towards increasing endurance and a significant increase (by 10%) in both succinate dehydrogenase activity and the percentage of muscle fibers containing slow myosin heavy chain (MHC) isoforms. At the same time, the proportion of fibers reacting with the antibody against fast MHC isoforms decreased by 12%. In group 1, the maximum voluntary force (MVF) significantly decreased, the volume of m. quadriceps femoris (as measured by magnetic resonance imaging) remained unchanged, and the size of the fast fibers slightly decreased (by 11%). In group 2, no significant decrease in the MVF was observed, while there was a significant increase in muscle volume and the cross-sectional area of muscle fibers.     

Mn-peroxidase from Pleurotus ostreatus: The action on the lignin

Summary Three Mn-peroxidases from Pleurotus ostreatus have been isolated and purified. Mn-peroxidase III was homogeneous by isoelectrofocusing and electrophoresis. Isolated Mn-peroxidase isoenzymes were able to depolymerise lignosulfonates pretreated with ozone. Ozone caused significant alterations of lignosulfonate molecular size distribution resulting in appearance of two fractions of destruction products.     

Evaluation of the efficiency of neoadjuvant chemotherapy in patients with breast cancer from the results of magnetic resonance imaging

The immediate efficiency of neoadjuvant chemotherapy was analyzed in 16 patients with Stages IIb-IIIb breast cancer, by applying magnetic resonance imaging. The latter allows the time course of tumor changes and the efficiency of neoadjuvant chemotherapy to be estimated with high accuracy.     

Engineering the pH-optimum of activity of the GH12 family endoglucanase by site-directed mutagenesis

Endo-1,4-β-glucanase from Penicillium verruculosum (PvEGIII) belongs to family 12 of glycoside hydrolases (GH12). Analysis of the enzyme 3D model structure showed that the amino acid residue Asp98 may directly affect the pH-profile of enzyme activity since it is located at the distance of hydrogen bond formation from Glu203 that plays the role of a general acid in catalysis. The gene encoding the PvEGIII was cloned into Escherichia coli. After the deletion of two introns, a plasmid construction was obtained allowing the PvEGIII expression in E. coli. Using site-directed mutagenesis, the Asp98Asn mutant of the PvEGIII was obtained. Both the wild type and mutant PvEGIIIs were expressed in E. coli with a yield of up to 1 g/L and then isolated in a highly purified form. The enzyme specific activity against soluble carboxymethylcellulose was not changed after a single amino acid substitution. However, the pH-optimum of activity of the mutant PvEGIII was shifted from pH 4.0 to 5.1, compared to the wild type enzyme. The shift in the enzyme pH-optimum to more neutral pH was also observed on insoluble cellulose, in the process of enzymatic depigmentation of denim fabric. Similar situation featuring the effect of the Asp/Asn residue, located near the Glu catalytic residue, on the enzyme activity pH-profile has previously been described for xylanases of the GH11 family. Thus, the glycoside hydrolases belonging to the GH11 and GH12 families function by a rather similar mechanism of catalysis.     

A product inhibition study of cellulases from Trichoderma longibrachiatum using dyed cellulose

Amorphous acid-swollen cellulose dyed with Reactive Orange was used to determine the relevant inhibition constants of cellulases from Trichoderma longibrachiatum by cellulose hydrolysis products (glucose and cellobiose). The method is based on the initial rate of increasing the hydrolysate absorbance (A_490mn) in the presence of added product. On adding glucose, the initial rate of glucose formation from cellulose and the rate of dye release were lower than the relevant rates in the absence of added product; however, the rate of cellobiose formation did not change. On the other hand, added cellobiose inhibited the rate of cellobiose formation from dyed cellulose and the rate of increase of the hydrolysate absorbance but did not affect the glucose formation. The constants of competitive inhibition of cellulases by glucose and cellobiose were 0.072 and 0.012 M, respectively. These inhibition parameters differed from those obtained from the analysis of the progress kinetics for extended reaction times.     

Regulatory activity of heterologous gene-activator <Emphasis Type="Italic">xlnR</Emphasis> of <Emphasis Type="Italic">Aspergillus niger</Emphasis> in <Emphasis Type="Italic">Penicillium canescens</Emphasis>

The gene encoding the xlnR xylanolytic activator of the heterologous fungus Aspergillus niger was incorporated into the Penicillium canescens genome. Integration of the xlnR gene resulted in the increase in a number of activities, i.e. endoxylanase, β-xylosidase, α-L-arabinofuranosidase, α-galactosidase, and feruloyl esterase, compared to the host P. canescens PCA 10 strain, while β-galactosidase, β-glucosidase, endoglucanase, and CMCase activities remained constant. Two different expression constructs were developed. The first consisted of the nucleotide sequence containing the mature P. canescens phytase gene under control of the axhA promoter region gene encoding A. niger (1,4)-β-D-arabinoxylan-arabinofuranohydrolase. The second construct combined the P. canescens phytase gene and the bgaS promoter region encoding homologous β-galactosidase. Both expression cassettes were transformed into P. canescens host strain containing xlnR. Phytase synthesis was observed only for strains with the bgaS promoter on arabinose-containing culture media. In conclusion, the bgaS and axhA promoters were regulated by different inducers and activators in the P. canescens strain containing a structural tandem of the axhA promoter and the gene of the xlnR xylanolytic activator.     

Study of the impact of intramyocardial implantation of stem cells on myocardial perfusion and contractility in patients with coronary heart disease concurrent with postinfarct cardiosclerosis and chronic heart failure

OBJECTIVE: to study of intramyocardial implantation of cultured bone marrow stem cells on myocardial perfusion and contractility in the surgical treatment of patients with coronary heart disease (CHD) and chronic heart failure (CHF), by synchronized single-photon emission computed tomography (SSPECT) of the myocardium. SUBJECTS AND METHODS: The study included 11 patients. Intramyocardial injection of cell injections into the myocardial periscarring areas was made at coronary bypass surgery. All the patients underwent 99mTc myocardial SSPECT MIBI before and 3, 6, 12 months after surgery. RESULTS AND CONCLUSIONS: Implantation of bone marrow stem cells into the left ventricular myocardium favorably affects left ventricular remodeling and contributes to the improvement of myocardial perfusion and contractility, as evidenced by 99mTc.     

Application of neutral-alkaline pectate lyases to cotton fabric boil off

Commercial and pilot pectate lyase preparations (EC 4.2.2.2) have been compared. They differ in their effect on pectins with different esterification degrees (ED). The activity of the pilot preparation with respect to a substrate with ED = 70% is tenfold lower than with respect to unesterified polygalacturonic acid. For commercial preparations, this activity ratio ranged within 1.5-2. At equal pectate lyase activities, the commercial preparations better remove pectin from crude cotton fabric during its boil off. The laboratory preparation is more efficient for improving the capillarity (wettability) of the fabric owing to the cooperative effect of the pectate lyase, cellulase, and hemicellulase present in the preparation.