Generation and characterization of air micro‐bubbles in highly hydrophobic capillaries

2021 ◽  
Author(s):  
Charly Renard ◽  
Laurent Leclercq ◽  
Hervé Cottet
Keyword(s):  
Highly Hydrophobic

scholarly journals Molecular cloning and analysis of l(1)ogre, a locus of Drosophila melanogaster with prominent effects on the postembryonic development of the central nervous system.

Genetics ◽  
1990 ◽  
Vol 126 (4) ◽  
pp. 1033-1044 ◽  
Author(s):  
T Watanabe ◽  
D R Kankel
Keyword(s):  
Central Nervous System ◽  
Nervous System ◽  
Postembryonic Development ◽  
P Element ◽  
Reading Frame ◽  
Isolation And Characterization ◽  
The Central Nervous System ◽  
Highly Hydrophobic ◽  
Conceptual Translation

Abstract Previous genetic studies have shown that wild-type function of the l(1)ogre (lethal (1) optic ganglion reduced) locus is essential for the generation and/or maintenance of the postembryonic neuroblasts including those from which the optic lobe is descended. In the present study molecular isolation and characterization of the l(1)ogre locus was carried out to study the structure and expression of this gene in order to gain information about the nature of l(1)ogre function and its relevance to the development of the central nervous system. About 70 kilobases (kb) of genomic DNA were isolated that spanned the region where l(1)ogre was known to reside. Southern analysis of a l(1)ogre mutation and subsequent P element-mediated DNA transformation mapped the l(1)ogre+ function within a genomic fragment of 12.5 kb. Northern analyses showed that a 2.9-kb message transcribed from this 12.5-kb region represented l(1)ogre. A 2.15-kb portion of a corresponding cDNA clone was sequenced. An open reading frame (ORF) of 1,086 base paris was found, and a protein sequence of 362 amino acids with one highly hydrophobic segment was deduced from conceptual translation of this ORF.

scholarly journals Sorbitol Transporter Expression in Apple Sink Tissues: Implications for Fruit Sugar Accumulation and Watercore Development

2005 ◽  
Vol 130 (2) ◽  
pp. 261-268 ◽  
Author(s):  
Zhifang Gao ◽  
Sastry Jayanty ◽  
Randolph Beaudry ◽  
Wayne Loescher
Keyword(s):  
Membrane Transport ◽  
Sour Cherry ◽  
Apium Graveolens ◽  
Sugar Accumulation ◽  
Isolation And Characterization ◽  
Photosynthetic Product ◽  
Highly Hydrophobic ◽  
Major Facilitator ◽  
Transporter Expression

In apple (Malus ×domestica Borkh.), where sorbitol is a primary photosynthetic product that is translocated throughout the plant, accumulation of sorbitol in sink cells appears to require an active carrier-mediated membrane transport step. Recent progress in isolation and characterization of genes for sorbitol transporters in sour cherry (Prunus cerasus L.) and mannitol transporters in celery (Apium graveolens L.) suggested that similar transporters may be present in apple tissues. A defect in these transporters could also explain the occurrence of the fruit disorder watercore, characterized by the accumulation of fluids and sorbitol in the apoplasmic free space. Our objectives therefore included isolation and characterization of genes for sorbitol transporters in apple tissues and comparisons of expression of transporter genes, especially in various sink tissues including watercored and non-watercored fruit tissues. We have isolated and characterized two sorbitol transporter genes, MdSOT1 and MdSOT2. Sequence analyses indicated that these are members of the major facilitator transporter superfamily that gives rise to highly hydrophobic integral membrane proteins. Heterologous expression and measurement of sorbitol uptake in yeast indicated that these are specific and with high affinities for sorbitol, with Kms for sorbitol of 1.0 and 7.8 mm for MdSOT1 and MdSOT2, respectively. Sorbitol transporter expression was evident in all sink tissues tested with the exception of watercore-affected fruit tissues. Sorbitol accumulation in apple sink tissues thus involves an apoplasmic active membrane transport step and watercore results from a defect in that process.

Purification of heat shock protein 90 from calf uterus and rat liver and characterization of the highly hydrophobic region

1989 ◽  
Vol 992 (1) ◽  
pp. 1-8 ◽  
Author(s):  
Masaomi Iwasaki ◽  
Hiroyuki Saito ◽  
Masahide Yamamoto ◽  
Kenneth S. Korach ◽  
Tsuneyoshi Hirogome ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Rat Liver ◽  
Heat Shock Protein 90 ◽  
Hydrophobic Region ◽  
Highly Hydrophobic

Characterization of the KstR-dependent promoter of the gene for the first step of the cholesterol degradative pathway in Mycobacterium smegmatis

Microbiology ◽  
2011 ◽  
Vol 157 (9) ◽  
pp. 2670-2680 ◽  
Author(s):  
Iria Uhía ◽  
Beatriz Galán ◽  
Francisco Javier Medrano ◽  
José Luis García
Keyword(s):  
Mycobacterium Smegmatis ◽  
Transcription Start ◽  
Promoter Regions ◽  
Degradative Pathway ◽  
Terminal Domain ◽  
Heterologous System ◽  
Highly Hydrophobic ◽  
Extension Analysis

The KstR-dependent promoter of the MSMEG_5228 gene of Mycobacterium smegmatis, which encodes the 3-β-hydroxysteroid dehydrogenase (3-β HSDMS) responsible for the first step in the cholesterol degradative pathway, has been characterized. Primer extension analysis of the P5228 promoter showed that the transcription starts at the ATG codon, thus generating a leaderless mRNA lacking a 5′ untranslated region (5′UTR). Footprint analyses demonstrated experimentally that KstR specifically binds to an operator region of 31 nt containing the quasi-palindromic sequence AACTGGAACGTGTTTCAGTT, located between the −5 and −35 positions with respect to the transcription start site. This region overlaps with the −10 and −35 boxes of the P5228 promoter, suggesting that KstR represses MSMEG_5228 transcription by preventing the binding of RNA polymerase. Using a P5228 –β-galactosidase fusion we have demonstrated that KstR is able to work as a repressor in a heterologous system like Escherichia coli. A 3D model of the KstR protein revealed folding typical of TetR-type regulators, with two domains, i.e. a DNA-binding N-terminal domain and a regulator-binding C-terminal domain composed of six helices with a long tunnel-shaped hydrophobic pocket that might interact with a putative highly hydrophobic inducer. The finding that similar P5228 promoter regions have been found in all mycobacterial strains examined, with the sole exception of Mycobacterium tuberculosis, provides new clues about the role of cholesterol in the pathogenicity of this micro-organism.

Isolation and Characterization of a Highly Hydrophobic New Bacteriocin (Gassericin A) fromLactobacillus gasseriLA39

1994 ◽  
Vol 58 (7) ◽  
pp. 1218-1221 ◽  
Author(s):  
Yasushi Kawai ◽  
Tadao Saito ◽  
Takahiro Toba ◽  
Shantanu K. Samant ◽  
Takatoshi Itoh
Keyword(s):  
Isolation And Characterization ◽  
Highly Hydrophobic

scholarly journals Reconstitution of cytochrome c oxidase in phospholipid vesicles containing polyvinylic polymers

1989 ◽  
Vol 257 (3) ◽  
pp. 783-787 ◽  
Author(s):  
P Sarti ◽  
G Antonini ◽  
F Malatesta ◽  
B Vallone ◽  
S Villaschi ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Functional Characterization ◽  
Respiratory Control ◽  
Phospholipid Vesicles ◽  
Lipid Phase ◽  
Protein Orientation ◽  
Highly Hydrophobic ◽  
Polymer Interaction

Cytochrome c oxidase was reconstituted in phospholipid vesicles in the presence of highly hydrophobic poly(vinyl alkanoate) polymers. Electron-microscopy observations demonstrated that polymer interaction with the lipid phase induces vesicles to adopt smaller diameters than those typical of standard proteoliposomes. Functional characterization of these polymer-proteoliposome structures indicates that the reconstitution of the enzyme proceeds efficiently without causing either scrambling of the protein orientation in the membrane or loss of respiratory control. A clear dependence of respiratory control ratio on vesicle size was also demonstrated, which is in agreement with a previous model proposed for control of activity of cytochrome c oxidase vesicles [Brunori, Sarti, Colosimo, Antonini, Malatesta, Jones & Wilson (1985) EMBO J. 4, 2365-2368].

Genetic analysis of microcin H47 immunity

1998 ◽  
Vol 44 (7) ◽  
pp. 692-697 ◽  
Author(s):  
Eliana Rodríguez ◽  
Magela Laviña
Keyword(s):  
Gene Fusion ◽  
Genetic System ◽  
Cellular Membrane ◽  
Peptide Analysis ◽  
Extracellular Medium ◽  
Hybrid Proteins ◽  
Site Of Action ◽  
Membrane Peptide ◽  
Highly Hydrophobic

Microcin H47 is a bactericidal antibiotic produced by a natural Escherichia coli isolate. The genetic system encoding microcin production and immunity consists of at least seven clustered genes. Four of these are devoted to microcin biosynthesis and two genes are required for its secretion into the extracellular medium. The product of the seventh gene, mchI, determines the cell's self-immunity. This gene was shown to encode a highly hydrophobic 69-residue peptide. Analysis of the MchI amino acid sequence, as well as the characterization of MchI–PhoA hybrid proteins, indicated that the microcin immunity product is probably exported out of the cytoplasm and remains an integral membrane peptide. This localization of the immunity peptide points to the cellular membrane as the site of action of microcin H47. Key words: microcin H47, microcin immunity, phoA gene fusion, membrane peptide.

Synthesis and biophysical characterization of highly hydrophobic transmembrane peptides

2006 ◽  
pp. 383-384
Author(s):  
Stefano Pegoraro ◽  
Simon Hellstern ◽  
Ariel Lustig ◽  
Sabine Frank ◽  
Jürgen Engel ◽  
...  
Keyword(s):  
Biophysical Characterization ◽  
Transmembrane Peptides ◽  
Highly Hydrophobic
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