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  • 1
    Electronic Resource
    Electronic Resource
    Differential tolerance to dietary amino acid-induced changes in aggressive behavior and locomotor activity in mice (1979)
    Springer
    Psychopharmacology 66 (1979), S. 301-308 
    Details
    ISSN: 1432-2072
    Keywords: Precursor amino acids ; Diet supplements ; Aggressive behavior ; Motor activity ; Norepinephrine ; Dopamine ; Serotonin ; Tolerance
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Male albino mice were maintained on a semisynthetic 12% casein protein diet for 2 weeks, then switched to diets modified by the addition of a 4% L-amino acid supplement (L-tyrosine, L-phenylalanine, and L-tryptophan) or 4% casein (control). Territorial-induced aggressive behavior increased following 1 week on the amino acid supplements, especially after tyrosine, but an apparent tolerance developed to these effects after 5 weeks on the amino acid supplements. Locomotor activity also increased following 1 week on the supplements, most notably after phenylalanine alone or in combination with tyrosine, and these effects tended to persist after 5 weeks on the supplements. Endogenous whole brain levels of dopamine, norepinephrine, serotonin, 5-hydroxyindoleacetic acid, tyrosine, phenylalanine, and tryptophan showed no tolerance to increased concentrations of brain catecholamines and indoleamines over the 5-week period, and no clear relation between the concentrations of these monoamines and the behavioral changes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00428324
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  • 2
    Electronic Resource
    Electronic Resource
    Differences in alkaline earth stimulation of neurotransmitter release from isolated brain synaptosomes (1978)
    Springer
    Naunyn-Schmiedeberg's archives of pharmacology 301 (1978), S. 175-179 
    Details
    ISSN: 1432-1912
    Keywords: Neurotransmitter ; GABA ; Norepinephrine ; Calcium ; Synaptosome
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary In the presence of 15 or 55 mM K+ buffer (calcium-deficient), pulses of the alkaline earths (Ca2+, Sr2+, Ba2+) stimulated secretion of previously accumulated [14C]GABA and [3H]norepinephrine (NE). For a 1 mM alkaline earth pulse in the presence of 15 mM K+, both GABA and NE release were ordered Ba2+〉Sr2+〉Ca2+. On the other hand, in 55 mM K+ the ordering was Ba2+〉Sr2+∼Ca2+. The change in ordering resulted from an increase in Ca-dependent release at higher K+. In fact, Ba-dependent release was smaller in 55 mM K+ solution than in 15 mM K+ solution. D-600 (10 μM), an antagonist of calcium influx, decreased both Ca- and Ba-dependent release of [14C]-GABA and [3H]NE in 15 mM K+ buffer. D-600 inhibited Ca-dependent release 60–70% whereas Ba-dependent release was inhibited only 30–45%. A CaCl2 (1 mM), BaCl2 (1 mM) or KCl (30 mM) pulse in 15 mM K+ buffer increased both [14C]GABA and endogenous GABA release. The Ba2+ pulse released more [14C] and endogenous GABA than did the Ca2+ pulse. The 30 mM KCl pulse released less [14C] and endogenous GABA than did either the Ba2+ or the Ca2+ pulse. However, the specific activity of the K-induced release was significantly higher than the specific activity of either Ca- or Ba-dependent GABA release. In substituting for Ca2+, Ba2+ may gain intracellular access to stimulus-secretion coupling processes via permeation at both Ca2+ and K+ ionophores.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00507034
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  • 3
    Electronic Resource
    Electronic Resource
    Alkaline phosphatase-somatostatin hybrid proteins as probes for somatostatin-14 receptors (1992)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 14 (1992), S. 1-9 
    Details
    ISSN: 0887-3585
    Keywords: protein engineering ; cassette mutagenesis ; peptide hormone ; molecular modeling ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: By inserting appropriate peptide ligands into surface loops on globular proteins, we expect to develop probes for the location, accessibility, and steric and electrostatic environment of these ligand-binding sites on their membrane-bound receptors. Three residues in a loop on the surface of E. coli alkaline phosphatase were substituted by an 18-residue peptide containing the receptor-binding segment of somatostatin-14 without significantly affecting the catalytic properties of the enzyme. This hybrid protein was then used to investigate the ligand-binding site of somatostatin receptors. Tryptic cleavage of the hybrid protein within the inserted sequence, and binding of the hybrid protein to antisomatostatin antibodies demonstrated the surface accessibility of the guest peptide. Both the wild-type enzyme and the hormone-enzyme hybrid displaced 125I-labeled somatostatin from rat brain membrane receptors only at high concentrations. How-ever, chemical cationization of the hybrid protein, which again did not disturb the phosphatase activity, enhanced its receptor-binding potency to a level only 23 times lower than that of somatostatin itself and 280 times higher than that of the cationized wild-type protein. This alkaline phosphatase/somatostatin hybrid protein appears, therefore, to be a suitable starting point for the development of probes for the steric and electrostatic environment of the ligand-binding site of somatostatin receptors. © 1992 Wiley-Liss, Inc.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/prot.340140103
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  • 4
    Electronic Resource
    Electronic Resource
    Reaction path and free energy calculations of the transition between alternate conformations of HIV-1 proteaseThe content of this publication does not necessarily reflect the views or policies of the Department of Health and Human Services, nor does mention of trade names, commercial products, or organization imply endorsement by the U.S. Government. (1998)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 32 (1998), S. 7-16 
    Details
    ISSN: 0887-3585
    Keywords: conformational change ; free energy calculations ; HIV protease ; molecular dynamics simulations ; protein structure ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: Two different structures of ligand-free HIV protease have been determined by X-ray crystallography. These structures differ in the position of two 12 residue, β-hairpin regions (or “flaps”) which cap the active site. The movements of the flaps must be involved in the binding of substrates since, in either conformation, the flaps block the binding site. One of these structures is similar to structures of the ligand-bound enzyme; however, the importance of both structures to enzyme function is unclear. This transformation takes place on a time scale too long for conventional molecular dynamics simulations, so the process was studied by first identifying a reaction path between the two structures and then calculating the free energy along this path using umbrella sampling. For the ligand-free enzyme, it is found that the two structures are nearly equally stable, with the ligand-bound-type structure being less stable, consistent with X-ray crystallography data. The more stable open structure does not have a lower potential energy, but is stabilized by entropy. The transition occurs through a collapse and reformation of the β-sheet structure of the conformationally flexible, glycine-rich flap ends. Additionally, some problems in studying conformational changes in proteins through the use of a single reaction path are addressed. Proteins 32:7-16, 1998. © 1998 Wiley-Liss, Inc.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Single-stranded DNA binding proteins (SSBs) from prokaryotic transmissible plasmids (1991)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 9 (1991), S. 120-134 
    Details
    ISSN: 0887-3585
    Keywords: plasmid SSBs ; protein and DNA sequence ; single-stranded DNA binding proteins ; helix destabilizing proteins ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: The DNA and protein sequences of single-stranded DNA binding proteins (SSBs) encoded by the plP71a, plP231a, and R64 conjugative plasmids have been determined and compared to Escherichia coli SSB and the SSB encoded by F-plasmid. Although the amino acid sequences of all of these proteins are highly conserved within the NH2-terminal two-thirds of the protein, they diverge in the COOH-terminal third region. A number of amino acid residues which have previously been implicated as being either directly or indirectly involved in DNA binding are conserved in all of these SSBs. These residues include Trp-40, Trp-54, Trp-88, His-55, and Phe-60. On the basis of these sequence comparisons and DNA binding studies, a role for Tyr-70 in DNA binding is suggested for the first time. Although the COOH-terminal third of these proteins diverges more than their NH2-terminal regions, the COOH-terminal five amino acid residues of all five of these proteins are identical. In addition, all of these proteins share the characteristic property of having a protease resistant, NH2-terminal core and an acidic COOH-terminal region. Despite the high degree of sequence homology among the plasmid SSB proteins, the F-plasmid SSB appears unique in that it was the only SSB tested that neither bound well to poly(dA) nor was able to stimulate DNA polymerase III holoenzyme elongation rates. Poly [d(A-T)] melting studies suggest that at least three of the plasmid encoded SSBs are better helix-destabilizing proteins than is the E. coli SSB protein.
    Additional Material: 10 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/prot.340090206
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  • 6
    Electronic Resource
    Electronic Resource
    Electrochemical observations in microbiological processes. Growth of Thiobacillus thiooxidans. I (1965)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 7 (1965), S. 471-490 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The growth of Thiobacillus Thiooxidans, utilizing sulfur in three media, was studied by observing changes in halfcell emf, bacterial cell count, and acid production, all as a function of time. A comparison of the biological halfcell emf with comparable control halfcells reveals that T. thiooxidans makes an electrochemical contribution to halfcell voltage. A change from the more complex medium of Skerman's mineral salts to ATCC allowed a clearer delineation of the ability of T. thiooxidans to make an electrochemical contribution. Reproducible biological halfcell emf's were obtained when the ferrous sulfate was removed from the ATCC medium. One halfcell, consisting of T. thiooxidans utilizing sulfur in ATCC, was observed over a 111-day period. During this time, the initial halfcell voltage of -0.35 V. decreased to a value of -0.64 V. (hydrogen emf series). T. thiooxidans, in utilizing sulfur, produces only sulfate ion, thereby simplifying the identification of an electrochemical contribution during growth.
    Additional Material: 12 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260070404
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  • 7
    Electronic Resource
    Electronic Resource
    Removal of chill haze from beer with papain immobilized on chitin (1977)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 19 (1977), S. 1895-1897 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Additional Material: 1 Tab.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260191213
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  • 8
    Electronic Resource
    Electronic Resource
    Effect of surfactant and particle size reduction on hydrolysis of deinking sludge and nonrecyclable newsprint (1995)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 45 (1995), S. 239-244 
    Details
    ISSN: 0006-3592
    Keywords: cellulase ; newsprint ; deinking sludge ; surfactant ; hydrolysis ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Disposal of sludge from deinking mills represents a significant proportion of operating costs. Bioconversion of the cellulosic fraction of deinking sludge (DIS) to ethanol greatly reduces disposal costs while producing an environmentally friendly fuel. In this study, the cellulosic fraction of newsprint and deinking sludge was hydrolysed to produce fermentable sugars. For newsprint, a particle size of 1 to 1.5 mm provided optimal reaction rates in batch reactors over practical hydrolysis times, and reducing sugar concentrations as high as 35 g/L could be achieved using a fed-batch reactor configuration. For both newsprint and DIS, the hydrolysis rate increased nonlinearly with enzyme loading. Tween-80 only marginally improved sugar production but was able to release sugars from cellulosic substrates in the absence of lytic enzymes, in an amount proportional to the surfactant concentration and the substrate particle size. DIS was relatively recalcitrant to enzymatic hydrolysis, possibly due in part to inhibition by hydrophobic constituents. © 1995 John Wiley & Sons, Inc.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260450308
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  • 9
    Electronic Resource
    Electronic Resource
    Assay of proteolytic activity by ultrafiltration (1982)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 24 (1982), S. 999-1006 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260240422
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  • 10
    Electronic Resource
    Electronic Resource
    Simultaneous saccharification and extractive fermentation of cellulosic substrates (1996)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 49 (1996), S. 504-511 
    Details
    ISSN: 0006-3592
    Keywords: cellulose ; cellulase ; simultaneous saccharification and extractive fermentation ; ethanol ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Alcohol fermentation has traditionally been carried out in aqueous environments because of the ready solubility of reactant (sugar) and product (ethanol). However, extraction of the product ethanol into a nonmiscible phase can result in kinetic benefits due to reduced inhibition of the fermentation reactions. In this study, we report the development of a novel simultaneous saccharification and extractive fermentation (SSEF) process. Ethanol productivity was increased by up to 65% over conventional (nonextractive) fed-batch simultaneous saccharification systems when calculated on the basis of aqueous phase volume. The amount of water required for SSEF reactions was dramatically reduced from that required for conventional SSF. In batch SSEF reactors with 2.5% aqueous phase, 50% conversion of 25% (aqueous phase concentration) Solka Floc could be achieved in 48 h using 2 FPU/g cellulase. © 1996 John Wiley & Sons, Inc.
    Additional Material: 10 Ill.
    Type of Medium: Electronic Resource
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