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  • Humans  (503)
  • Biochemistry and Biotechnology  (351)
  • Physical Chemistry
  • 1990-1994  (760)
  • 1975-1979  (222)
  • 1
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 40 (1992), S. 1435-1439 
    ISSN: 0006-3592
    Keywords: osmotic pressure ; osmotic stress ; osmotolerance ; physiological state ; yeasts ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The variation rate of the osmotic pressure increase was found to have a great effect on the viability of yeasts subjected to hyperosmotic stress. A low intensity of the increase rate of osmotic pressure could maintain an important viability of the cells (about 90 to 100%) even for very high levels of osmotic pressure (about 108 Pa). The viability level was found to be highly dependent on the physiological state of the cells: Variations in the properties of the cell membrane were supposed to be involved in such a dependence. © 1992 John Wiley & Sons, Inc.
    Additional Material: 4 Ill.
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  • 2
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 38 (1991), S. 552-556 
    ISSN: 0006-3592
    Keywords: stirring ; turbulence ; shear effects ; lysine fermentation ; Brevibacterium flavum ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Excess turbulence caused by high-intensity stirring inhibited microbial growth and metabolism. In stirred tank bioreactors, the growth rate and lysine biosynthesis decreased in Brevibacterium flavum beyond 900 rpm, the growth rate of Trichoderma reesei on wheat straw beyond 150 rpm, and the growth rate of Saccharomyces cerevisae beyond 800 rpm. The term turbohypobiosis was introduced to describe this inhibition. Turbohypobiosis was characterized by a stress factor Fstr expressing the interaction of medium flow with microbial cells in local turbulent zones, dependent on the energy distribution of the stirring regime. Lysine synthesis was inhibited at significantly lower Fstr values than the growth of B. flavum. The main reason for the inhibition was shear effects causing decreased adenosine triphosphate (ATP) generation, lower O2 uptake, and lower specific growth rate of bacteria.
    Additional Material: 6 Ill.
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  • 4
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    International Journal of Chemical Kinetics 8 (1976), S. 23-24 
    ISSN: 0538-8066
    Keywords: Chemistry ; Physical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
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  • 5
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    International Journal of Chemical Kinetics 11 (1979), S. 175-185 
    ISSN: 0538-8066
    Keywords: Chemistry ; Physical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Relaxation rates for O2(1Σg+) by nonradiative pathways have been determined using the fast-flow technique. O2(1Σg+) is formed from O2(1Δg) by an energy pooling process. O2(1Δg) is generated by passing purified oxygen through a microwave discharge. Oxygen atoms are removed by distilling mercury vapor through the discharge zone. It has been observed that the wall loss rate for O2(1Σg+) decreases with increasing pressure of oxygen and thus appears to be diffusion controlled. Quenching rate constants for O2, N2, and He have been determined and found to be (1.5 ± 0.1) × 104, (1.0 ± 0.05) × 106 and (1.2 ± 0.1) × 105 l./mol·sec, respectively.
    Additional Material: 6 Ill.
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  • 6
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    International Journal of Chemical Kinetics 25 (1993), S. 521-537 
    ISSN: 0538-8066
    Keywords: Chemistry ; Physical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: A laser flash photolysis-long path absorption technique has been employed to study the kinetics of the reaction products as a function of temperature (248-346 K), pressure (16-800 torr), and buffer gas identity (N2, CF4). The reaction is found to be in the falloff regime between third and second-order over the entire range of conditions investigated. This is the first study where temperature-dependent measurements of k1(P, T) have been reported at pressures greater than 12 torr; hence, our results help constrain choices of k1(P, T) for use in models of lower stratospheric BrOx chemistry. Approximate falloff parameters in a convenient form for atmospheric modeling are derived. © 1993 John Wiley & Sons, Inc.
    Additional Material: 9 Ill.
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  • 7
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    International Journal of Chemical Kinetics 25 (1993), S. 805-817 
    ISSN: 0538-8066
    Keywords: Chemistry ; Physical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: This article describes the first direct determination of the rate coefficient for the self-reaction between two NO3 radicals. A laser photolysis technique was used to generate NO3, and time-resolved decays of NO3 were followed after stopping the photolysis. The products of the reaction are inferred to be NO2 and O2. The derived rate coefficient at room temperature for the self-reaction of (2.3 ± 0.8) ×10-16 cm3 molecule-1s-1 is in excellent agreement with the only other data, which were obtained in an indirect study. Consideration is given to the magnitude and influence of secondary chemistry and to the participation of FO in the chemistry of the NO3 buildup phase. The studies were conducted over a pressure range of 8 to 100 torr in helium. No clear pressure dependence was observed, and some tentative inferences are drawn both from this result and from the absolute magnitude of the rate coefficient about the mechanism of the reaction. There is apparently no role for the reaction in the chemistry of the atmosphere. © 1993 John Wiley & Sons, Inc.
    Additional Material: 7 Ill.
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  • 8
    Publication Date: 1991-05-03
    Description: Although bladder cancers are very common, little is known about their molecular pathogenesis. In this study, invasive bladder cancers were evaluated for the presence of gene mutations in the p53 suppressor gene. Of 18 tumors evaluated, 11 (61 percent) were found to have genetic alterations of p53. The alterations included ten point mutations resulting in single amino acid substitutions, and one 24-base pair deletion. In all but one case, the mutations were associated with chromosome 17p allelic deletions, leaving the cells with only mutant forms of the p53 gene products. Through the use of the polymerase chain reaction and oligomer-specific hybridization, p53 mutations were identified in 1 to 7 percent of the cells within the urine sediment of each of three patients tested. The p53 mutations are the first genetic alterations demonstrated to occur in a high proportion of primary invasive bladder cancers. Detection of such mutations ex vivo has clinical implications for monitoring individuals whose tumor cells are shed extracorporeally.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sidransky, D -- Von Eschenbach, A -- Tsai, Y C -- Jones, P -- Summerhayes, I -- Marshall, F -- Paul, M -- Green, P -- Hamilton, S R -- Frost, P -- CA09071/CA/NCI NIH HHS/ -- CA43460/CA/NCI NIH HHS/ -- CA49758/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1991 May 3;252(5006):706-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Oncology, Johns Hopkins University, Baltimore, MD 21231.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2024123" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Base Sequence ; Chromosome Deletion ; Chromosomes, Human, Pair 17 ; *Genes, p53 ; Humans ; Molecular Sequence Data ; *Mutation ; Nucleic Acid Hybridization ; Oligonucleotide Probes ; Polymerase Chain Reaction ; Urinary Bladder Neoplasms/*genetics/urine ; Urine/cytology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 9
    Publication Date: 1991-02-01
    Description: Multiple mutations in the gene responsible for cystic fibrosis are located within a region predicted to encode a nucleotide-binding fold in the amino terminal half of the cystic fibrosis transmembrane conductance regulator protein. A 67-amino acid peptide (P-67) that corresponds to the central region of this putative nucleotide binding site was chemically synthesized and purified. This peptide bound adenine nucleotides. The apparent dissociation constants (Kd's) for the trinitrophenyl (TNP) adenine nucleotides, TNP-adenosine triphosphate, TNP-adenosine diphosphate, and TNP-adenosine monophosphate, were 300 nanomolar, 200 nanomolar, and greater than 1 micromolar, respectively. The Kd for adenosine triphosphate was 300 micromolar. Circular dichroism spectroscopy was used to show that P-67 assumes a predominantly beta sheet structure in solution, a finding that is consistent with secondary structure predictions. On the basis of this information, the phenylalanine at position 508, which is deleted in approximately 70 percent of individuals with cystic fibrosis, was localized to a beta strand within the nucleotide binding peptide. Deletion of this residue is predicted to induce a significant structural change in the beta strand and altered nucleotide binding.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Thomas, P J -- Shenbagamurthi, P -- Ysern, X -- Pedersen, P L -- CA 10951/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1991 Feb 1;251(4993):555-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD 21205.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1703660" target="_blank"〉PubMed〈/a〉
    Keywords: Adenine Nucleotides/*metabolism ; Amino Acid Sequence ; Binding Sites ; Chromatography, High Pressure Liquid ; Cystic Fibrosis/*genetics/metabolism ; Cystic Fibrosis Transmembrane Conductance Regulator ; Humans ; Membrane Proteins/*genetics/isolation & purification/metabolism ; Molecular Sequence Data
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 10
    Publication Date: 1991-12-20
    Description: Dimerization among transcription factors has become a recurrent theme in the regulation of eukaryotic gene expression. Hepatocyte nuclear factor-1 alpha (HNF-1 alpha) is a homeodomain-containing protein that functions as a dimer. A dimerization cofactor of HNF-1 alpha (DCoH) was identified that displayed a restricted tissue distribution and did not bind to DNA, but, rather, selectively stabilized HNF-1 alpha dimers. The formation of a stable tetrameric DCoH-HNF-1 alpha complex, which required the dimerization domain of HNF-1 alpha, did not change the DNA binding characteristics of HNF-1 alpha, but enhanced its transcriptional activity. However, DCoH did not confer transcriptional activation to the GAL4 DNA binding domain. These results indicate that DCoH regulates formation of transcriptionally active tetrameric complexes and may contribute to the developmental specificity of the complex.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mendel, D B -- Khavari, P A -- Conley, P B -- Graves, M K -- Hansen, L P -- Admon, A -- Crabtree, G R -- CA 09302/CA/NCI NIH HHS/ -- HD 07201/HD/NICHD NIH HHS/ -- HL 33942/HL/NHLBI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1991 Dec 20;254(5039):1762-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Stanford University, CA 94305.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1763325" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cell Nucleus/physiology ; Chromosome Deletion ; DNA-Binding Proteins/*metabolism ; Gene Library ; Hepatocyte Nuclear Factor 1 ; Hepatocyte Nuclear Factor 1-alpha ; Hepatocyte Nuclear Factor 1-beta ; Humans ; *Hydro-Lyases ; Liver/physiology ; Macromolecular Substances ; Mice ; Molecular Sequence Data ; *Nuclear Proteins ; Protein Biosynthesis ; RNA, Messenger/genetics ; Rabbits ; Rats ; Reticulocytes/metabolism ; Transcription Factors/genetics/*metabolism ; Transcription, Genetic
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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