Bands Corresponding (bands + corresponding)

Distribution by Scientific Domains


Selected Abstracts


Isolation and characterization of a Lactobacillus amylovorus mutant depleted in conjugated bile salt hydrolase activity: relation between activity and bile salt resistance

JOURNAL OF APPLIED MICROBIOLOGY, Issue 4 2000
J.P. Grill
Growth experiments were conducted on Lactobacillus amylovorus DN-112 053 in batch culture, with or without pH regulation. Conjugated bile salt hydrolase (CBSH) activity was examined as a function of culture growth. The CBSH activity increased during growth but its course depended on bile salts type and culture conditions. A Lact. amylovorus mutant was isolated from the wild-type strain of Lact. amylovorus DN-112 053 after mutagenesis with N-methyl-N,-nitro-N-nitrosoguanidine. An agar plate assay was used to detect mutants without CBSH activity. In resting cell experiments, the strain showed reduced activity. Differences between growth parameters determined for wild-type and mutant strains were not detected. Comparative native gel electrophoresis followed by CBSH activity staining demonstrated the loss of proteins harbouring this activity in the mutant. Four protein bands corresponding to CBSH were observed in the wild-type strain but only one was detected in the mutant. The specific growth rate of the mutant strain was affected more by bile salts than the wild-type strain. Nevertheless, bile was more toxic for the wild-type strain. In viability studies in the presence of nutrients, it was demonstrated that glycodeoxycholic acid exerted a higher toxicity than taurodeoxycholic acid in a pH-dependent manner. No difference was apparent between the two strains. In the absence of nutrients, the wild-type strain died after 2 h whereas no effect was observed for the mutant. The de-energization experiments performed using the ionophores nigericin and valinomycin suggested that the chemical potential of protons (Z,pH) was involved in Lactobacillus bile salt resistance. [source]


Novel identification of peripheral dopaminergic D2 receptor in male germ cells,

JOURNAL OF CELLULAR BIOCHEMISTRY, Issue 1 2007
Carola Otth
Abstract Dopamine is a recognized modulator in the central nervous system (CNS) and peripheral organ functions. The presence of peripheral dopamine receptors outside the CNS has suggested an intriguing interaction between the nervous system and other functional systems, such as the reproductive system. In the present study we analyzed the expression of D2R receptors in rat testis, rat spermatogenic cells and spermatozoa, in different mammals. The RT-PCR analysis of rat testis mRNA showed specific bands corresponding to the two dopamine receptor D2R (L and S) isoforms previously described in the brain. Using Western blot analysis, we confirmed that the protein is present in rat testis, isolated spermatogenic cells and also in spermatozoa of a range of different mammals, such as rat, mouse, bull, and human. The immunohistochemistry analysis of rat adult testis showed that the receptor was expressed in all germ cells (pre- and post-meiotic phase) of the tubule with staining predominant in spermatogonia. Confocal analysis by indirect immunofluorescence revealed that in non-capacitated spermatozoa of rat, mouse, bull, and human, D2R is mainly localized in the flagellum, and is also observed in the acrosomal region of the sperm head (except in human spermatozoa). Our findings demonstrate that the two D2 receptor isoforms are expressed in rat testis and that the receptor protein is present in different mammalian spermatozoa. The presence of D2R receptors in male germ cells implies new and unsuspected roles for dopamine signaling in testicular and sperm physiology. J. Cell. Biochem. 100: 141,150, 2007. 2006 Wiley-Liss, Inc. [source]


Purification and some properties of a cysteine proteinase from sorghum malt variety SK5912

JOURNAL OF THE SCIENCE OF FOOD AND AGRICULTURE, Issue 2 2004
Augustine C Ogbonna
Abstract A cysteine proteinase from sorghum malt variety SK5912 was purified by a combination of 4 M sucrose fractionation, ion-exchange chromatography on Q- and S-Sepharose (fast flow), gel filtration chromatography on Sephadex G-100 and hydrophobic interaction chromatography on Phenyl Sepharose CL-4B. The enzyme was purified 8.4-fold to give a 13.4% yield relative to the total activity in the crude extract and a final specific activity of 2057.1 U mg,1 protein. SDS,PAGE revealed two migrating protein bands corresponding to apparent relative molecular masses of 55 and 62 kDa, respectively. The enzyme was optimally active at pH 6.0 and 50 C, not influenced across a relatively broad pH range of 5.0,8.0 and retained over 60% activity at 70 C after 30-min incubation. It was highly significantly (P < 0.001) inhibited by Hg2+, appreciably (P < 0.01) inhibited by Ag+, Ba2+ and Pb2+ but highly significantly (P < 0.001) activated by Co2+, Mn2+ and Sr2+. The proteinase was equally highly significantly (P < 0.001) inhibited by both iodoacetate and p -chloromercuribenzoate and hydrolysed casein to give the following kinetic constants: Km = 0.33 mg ml,1; Vmax = 0.08 mol ml,1 min,1. Copyright 2004 Society of Chemical Industry [source]


Photoluminescence properties of GaAs nanowire ensembles with zincblende and wurtzite crystal structure

PHYSICA STATUS SOLIDI - RAPID RESEARCH LETTERS, Issue 7 2010
B. V. Novikov
Abstract Self-standing III,V nanowires (NWs) are promising building blocks for future optoelectronic devices such as LEDs, lasers, photodetectors and solar cells. In this work, we present the results of low temperature photoluminescence (PL) characterization of GaAs NWs grown by Au-assisted molecular beam epitaxy (MBE), coupled with the transmission electron microscopy (TEM) structural analysis. PL spectra contain exci- ton peaks from zincblende (ZB) and wurtzite (WZ) crystal structures of GaAs. The peaks are influenced by the quantum confinement effects. PL bands corresponding to the exciton emission from ZB and WZ crystal phases are identified, relating to the PL peaks at 1.519 eV and 1.478 eV, respectively. The obtained red shift of 41 meV for WZ GaAs should persist in thin NWs as well as in bulk materials. ( 2010 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim) [source]


The band structure of a layered Hg3TeCl4 crystal formed by energy states of HgCl2 and HgTe crystals

PHYSICA STATUS SOLIDI (B) BASIC SOLID STATE PHYSICS, Issue 8 2008
M. Sznajder
Abstract The ab-initio calculated band structure of a not as yet investigated orthorhombic Hg3TeCl4 crystal (Pbca, D152h) was analyzed by means of the elementary energy-bands concept. It was demonstrated that this band structure originates from that of a layered HgCl2 dielectric deformed by the presence of the HgTe structural elements. Further, it was revealed that the valence band of Hg3TeCl4 is composed of the 8-branch elementary energy bands corresponding to the actual Wyckoff position c (x, y, z) of D152h group that indicates the presence of ionic and covalent contributions to the chemical bonding in the crystal. The existence of Davydov splitting in the 8-branch elementary energy band situated in the low-energy range of the valence band was observed, which is typical for layered crystals with a weak interlayer interaction between translationally nonequivalent structural units. It was shown that the anisotropy of the electron and hole effective masses does not correspond to the macroscopic anisotropy of the crystal and an explanation of this behaviour was proposed. The obtained parameters of the crystal (direct energy gap Eg = 2.49 eV as well as values of the estimated electron effective masses) indicate that it could find an application in optoelectronics. ( 2008 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim) [source]


Effect of form anisotropy of silicon nanocrystals on birefringence and dichroism in porous silicon

PHYSICA STATUS SOLIDI (C) - CURRENT TOPICS IN SOLID STATE PHYSICS, Issue 6 2007
A. I. Efimova
Abstract Artificial anisotropic optical media based on nanostructured silicon formed by electrochemical porosifying of Si substrates are investigated. Strong birefringence and dichroism of surface silicon-hydrogen bonds vibrations are found in the infrared spectral range. A comprehensive analysis of the absorption bands corresponding to the deformation and stretching modes is performed. The experimental results are discussed in terms of an effective medium model, taking into account the morphological anisotropy of Si nanocrystals in porous Si layers. ( 2007 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim) [source]


Identification and partial characterization of selected proteolytic enzymes in the digestive system of giant freshwater Prawn Macrobrachium rosenbergii (De Man) Postlarvae

AQUACULTURE RESEARCH, Issue 5 2009
Mohamed Ayaz Hasan Chisty
Abstract Biochemical assays and substrate SDS-PAGE were conducted to partially characterize and identify various types of proteases present in the digestive tract of PL15 giant freshwater prawn (Macrobrachium rosenbergii). Casein hydrolytic assay of the enzyme extracts showed major proteolytic activities at pH 3.0, 6.0 and 9.0, while assay of preincubated enzyme extracts with phenylmethylsulphonyl fluoride (PMSF), a serine protease inhibitor produced a 33.17% reduction in alkaline protease activity. When specific inhibitors tosyl-lysine chloromethyl ketone and tosyl-phenylalanine chloromethyl ketone were used, they resulted in a reduction in activity of proteases in the enzyme extracts by 82.41% and 55.03%, respectively, confirming the presence of trypsin and chymotrypsin, while ethylenediamine tetraacetic acid produced protease activity reduction in 33.92% showing the presence of metalloproteases in the digestive tract of the prawn. Further characterization of the alkaline proteases using SDS-PAGE technique, after incubating the extract in the presence or absence of specific inhibitors, produced six bands corresponding to molecular masses of between 13.48 and 136.1 kDa; two trypsin bands of 13.48 and 36.4 kDa, three chymotrypsin bands in the range of 23.0,73.4 kDa and one for metalloprotease of 136.1 kDa, all of which were identified from a zymogram. This study suggests that protein digestion in M. rosenbergii is initiated by an acid protease followed by a combination of action of alkaline proteases: trypsin, chymotrypsin and metalloproteases. [source]