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  • Wiley-Blackwell  (14)
  • 1985-1989  (14)
  • 1
    Electronic Resource
    Electronic Resource
    Single-cell protein from methanol with Enterobacter aerogenes (1987)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 29 (1987), S. 355-357 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: An identifiedEnterobacter aerogenesutilizing methanol as a sole carbon source was studied for the optimization of biomass production and the reduction of its nucleic acid content. Results indicated that the highest yield and conversion were obtained at 0.5% methanol. The addition of seawater as a source of trace elements has an adverse effect. However, the addition of urea as source of nitrogen enhanced the growth of E. aerogenes. Heat shock at 60°C for 1 min followed by incubation at 50°C for 2 h caused 72.6% reduction in the nucleic acid.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260290310
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  • 2
    Electronic Resource
    Electronic Resource
    Stereochemical influences upon the opioid ligand activities of 4-alkyl-4-arylpiperidine derivatives (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Chirality 1 (1989), S. 202-208 
    Details
    ISSN: 0899-0042
    Keywords: opioid ligand ; 4-arylpiperidines ; conformation, NMR ; Chemistry ; Organic Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The synthesis and stereochemistry (configuration and preferred solute conformation) of some 4-alkyl (methyl, n-propyl, isobutyl)-4-(3-hydrxyphenyl)-1-methylpiperidines and corresponding 3-methyl diastereoisomeric pairs are reported, together with their in vivo and in vitro activities as opioid ligands. All potent agonists exhibit a preference for axial 4-aryl chair conformations when protonated, and stereochemical analogies with rigid opioids of the benzomorphan class are discussed. Antagonist properties are found in compounds with preference for equatorial 4-aryl chairs, notably the cis 3,4-dimethyl derivative.
    Additional Material: 3 Tab.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/chir.530010305
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  • 3
    Electronic Resource
    Electronic Resource
    Correlation between the distribution of smooth muscle or non muscle myosins and α-smooth muscle actin in normal and pathological soft tissues (1988)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 11 (1988), S. 260-274 
    Details
    ISSN: 0886-1544
    Keywords: cytoskeleton ; atheromatosis ; wound healing ; fibromatosis ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The distribution of smooth muscle (SM) and non muscle myosins was compared with that of α-SM actin in various normal and pathological tissues and in cultured cells by means of indirect immunofluorescence using a monoclonal antibody specific for α-SM actin [anti-αsm-1, Skalli et al., 1986b] and two polyclonal antibodies raised against bovine aortic myosin (ABAM) and human platelet myosin (AHPM), respectively.In normal tissues ABAM stained vascular and parenchymal smooth muscle cells (SMC), myoepithelial cells and myoid cells of the testis in a pattern similar to that reported by other authors with antisera raised against non vascular SM myosin. Cells stained with ABAM were always positive for anti-αsm-1. In human and experimental atheromatous plaques, most cells were positive for AHPM; a variable proportion was also stained for ABAM plus anti-αsm-1. Myofibroblasts from rat granulation tissue, Dupuytren's nodule and stroma from breast carcinoma were constantly positive for AHPM and negative for ABAM; however, myofibroblasts from Dupuytren's nodule and breast carcinoma were anti-αsm-1 positive. Early primary cultures of rat aortic SMC were positive for ABAM and anti-αsm-1 and became negative for ABAM and positive for AHPM after a few days in culture. They remained positive for AHPM and anti-αsm-1 after passages; the staining of AHPM and anti-αsm-1 appeared to be colocalized along the same stress fibers.These results may be relevant for the understanding of SMC function and adaptation, and show that in non malignant SMC proliferation, α-SM actin represents a more general marker of SM origin than SM myosin.
    Additional Material: 12 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970110405
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  • 4
    Electronic Resource
    Electronic Resource
    Binding of chemotactic peptide to the outer surface and to whole human spermatozoa with different affinity states (1988)
    New York, NY : Wiley-Blackwell
    Gamete Research 20 (1988), S. 233-239 
    Details
    ISSN: 0148-7280
    Keywords: human sperm ; membrane ; receptors ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Binding of N-formyl-methionyl-L-leucyl-[3H]phenylalanine (fML[3H]Ph) to human ejaculated spermatozoa and to its isolated plasma membrane was studied. Our data confirm the presence of specific receptors for f-MLPh in the human spermatozoa and suggest that whole spermatozoa receptors exist in two affinity states, one high-affinity, low-capacity specific receptor (Kd = 12.3 ± 0.5 nM, n = 22,285 ± 65,008 binding sites per sperm cell) and a second one (Kd = 700 ± 47 nM) that is not saturable, indicating a low-affinity, high-capacity nonspecific site. In contrast, sperm membrane showed only one class of binding site (Kd = 6.4 ± 0.12 nM), which was statistically different from that of the high-affinity binding site of intact spermatozoa. To explain this difference we discuss the possibility that first, the two binding affinities represent two interconvertible states of a single receptor population, which, depending on the metabolic activity of spermatozoa, may change its physicochemical properties; or second, they reflect two different processes, binding and/or transport into the spermatozoa.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/mrd.1120200213
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  • 5
    Electronic Resource
    Electronic Resource
    Heparin and glutathione: Physiological decondensing agents of human sperm nuclei (1989)
    New York, NY : Wiley-Blackwell
    Gamete Research 23 (1989), S. 39-47 
    Details
    ISSN: 0148-7280
    Keywords: nuclei decondensation ; thiol reagents ; reduced glutathione ; glycosaminoglycan ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: It has been proposed that reduced glutathione (GSH) or other thiol reagents may partici pate in the basic mechanism by which sperm-decondensing activity is accomplished. How ever, in vitro, these reagents seem to be inactive and require the presence of other chemi cals, usually detergents. Heparin binds specifically to the sperm membrane and provokes the decondensation of human sperm and the activation of DNA transcription and synthe sis. However, the concentrations at which these effects occur seem to be higher than those expected under physiological conditions. In the present study, thiol reagents at 10 mM concentration, either alone or combined, were completely ineffective in inducing any sig nificant nuclear decondensation after prolonged exposures (24 hr) of incubation. Heparin, 153.8 μM, was capable of inducing only a small increase in nuclear swelling. However, GSH at concentrations as low as 0.1 mM in combination with heparin induces deconden sation of human sperm nuclei in vitro. When GSH concentration was kept constant at 5 mM, nuclear decondensation was induced with heparin at concentrations as low as 11.6 μM, and a maximal decondensation (90%) was obtained with only 21.6 μM of heparin. The latter is more than ten times less than the minimal active concentration of heparin used alone.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/mrd.1120230105
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  • 6
    Electronic Resource
    Electronic Resource
    A rapid screening technique for identifying murine monoclonal antibodies to human apolipoprotein A-I isoforms by Western blot analysis (1987)
    Weinheim : Wiley-Blackwell
    Electrophoresis 8 (1987), S. 552-556 
    Details
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: A rapid method for determining the reactivity of murine monoclonal antibodies with apolipoprotein A-I (Apo A-I) isoforms has been developed. The method consists of a rapid (1-2 h) prescreening of fusion well culture fluids by using an automated immunofluorescent assay (IF A) to identify fusion well cultures producing monoclonal antibody against Apo A-I and high-density lipoprotein (HDL). Immediately following the IFA procedure, immunodetection of the reactivity pattern of selected fusion well culture fluids is determined by using transblotted isoforms of Apo A-I previously separated by isoelectric focusing. Strips are prepared and stored at 4 °C in protein containing blocking solution before use. Preselected culture fluids could be tested within 6 h for qualitative reactivity with Apo A-I isoforms. Using this procedure we selected several monoclonal antibody-producing cultures for further studies on HDL metabolism based on their differing reactivities with Apo A-I isoforms. This technique should be easily transferable to other laboratories for assessing proteins having multiple isoforms since the crucial steps of separation and blotting can be optimized and performed before actual testing for antibody reactivity.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150081203
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  • 7
    Electronic Resource
    Electronic Resource
    Polymerization and conformational studies of poly(trans-3-ethyl-D and L-proline) (1987)
    Bognor Regis [u.a.] : Wiley-Blackwell
    Journal of Polymer Science Part A: Polymer Chemistry 25 (1987), S. 2941-2952 
    Details
    ISSN: 0887-624X
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Poly(L-trans-3-ethylproline), L-PT3EP, and poly(D-trans-3-ethylproline), D-PT3EP, were prepared by ring opening polymerization of the corresponding N-carboxyanhydrides (NCA) using triethylamine as an initiator. Using circular dichroism spectroscopy, it was shown that the incorporation of an ethyl group at the 3 position of the pyrrolidine ring caused a noticeable change in the conformational behavior of the polymer in solution. The ethyl group limited to some extent rotation of the polymer chain around the C——CO bond and prevented the mutarotation between the two forms found in poly-L-proline polymers.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/pola.1987.080251102
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  • 8
    Electronic Resource
    Electronic Resource
    Synthesis, separation, and resolution of cis- and trans-3-ethylproline (1987)
    Bognor Regis [u.a.] : Wiley-Blackwell
    Journal of Polymer Science Part A: Polymer Chemistry 25 (1987), S. 3437-3458 
    Details
    ISSN: 0887-624X
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The synthesis, separation, and optical resolution of cis- and trans-3-ethylproline are described. Two different approaches were employed: (1) The Michael addition reaction of 2-pentenal with diethyl-N-carbobenzyloxyaminomalonate gave the intermediate 3-ethyl-5-hydroxy-N-benzyloxypyrrolidine. Hydrogenolysis of this intermediate followed by acid hydrolysis gave a mixture of cis- and trans-3-ethylproline. Separation of the isomers was accomplished by selective saponification of N-(p-toluenesulfonyl)-cis- and trans-3-ethylproline methyl esters using 0.25N methanolic sodium hydroxide. (2) The Michael condensation of diethyl acetamidomalonate with 2-pentenoic acid ethyl ether produced the intermediate 5,5-bis(ethoxycarbonyl)-4-ethylpyrrolidine. Partial saponification followed by decarboxylation afforded a mixture of cis- and trans-isomers of ethyl-3-ethylpyroglutamate. The diastereoisomers were separated using low temperature fractional crystallization. Reduction of these isomers and tosylation in situ afforded the corresponding N-(p-toluenesulfonyl)-cis- and trans-3-ethylprolinols. Chromic acid oxidation gave N-(p-toluenesulfonyl)-cis- and trans-3-ethylproline. Reaction of these tosylates with 30% hydrogen bromide in acetic acid gave cis- and trans-3-ethylproline. Both optically active isomers of D(+)-and L(-)-trans-3-ethylproline were successfully resolved using (+)-dibenzoyl-D-tartaric acid and (-)-dibenzoyl-L-tartaric acid as resolving agents. The absolute configurations of the optically active isomers were determined by circular dichroism spectroscopy.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/pola.1987.080251224
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  • 9
    Electronic Resource
    Electronic Resource
    Genetic evidence that the steroid-regulated trafficking of cell surface glycoproteins in rat hepatoma cells is mediated by glucocorticoid-inducible cellular components (1987)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 35 (1987), S. 271-284 
    Details
    ISSN: 0730-2312
    Keywords: glycoprotein trafficking variant ; mouse mammary tumor virus ; heterokaryons ; glucocorticoid receptor deficient variant ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: The biological control of posttranslational maturation and compartmentalization reactions that operate upon proteins during transport to their final cellular desti- nations is crucial for normal cellular function. Using the expression of mouse mammary tumor virus (MMTV) glycoproteins as sensitive probes in the viral- infected rat hepatoma cell line M1.54, we have discovered and documented a novel glucocorticoid-regulated trafficking pathway that controls the cell surface localization of MMTV glycoproteins. One complement-selected derivative of M1.54 cells, CR4, failed to compartmentalize cell surface MMTV glycoproteins in the presence of dexamethasone. To test genetically if this glycoprotein trafficking pathway is mediated by cellular or viral gene products, CR4 cells were fused with uninfected Fu5 rat hepatoma cells. Indirect immunofluorescence of CR4 × Fu5 heterokaryons revealed that Fu5 complemented the defect in CR4 only after exposure to 1 μM dexamethasone. The glucocorticoid inhibition of Fu5 proliferation was exploited to recover the receptor-deficient uninfected derivative EDR3 that expressed a 100-fold lower level of [3H]dexamethasone binding activity. Analysis of CR4 × EDR3 cell fusions by indirect immunofluorescence revealed that EDR3 cells complemented CR4 in a dexamethasone-dependent manner, suggesting that EDR3 supplied a functional trafficking component while CR4 provided a functional glucocorticoid receptor to the heterokaryons. Taken together, our results demonstrate that cellular-encoded glucocorticoid-inducible components mediate the regulated trafficking of cell surface MMTV glycoproteins.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcb.240350402
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  • 10
    Electronic Resource
    Electronic Resource
    Molecular and crystal structures of three monothiated analogues of the terminally blocked ala-aib-ala sequence of peptaibol antibiotics (1988)
    New York : Wiley-Blackwell
    Biopolymers 27 (1988), S. 747-761 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The molecular and crystal structures of three monothiated analogues of the blocked L-Ala-Aib-L-Ala sequence of peptaibol antibiotics, t-Boc-L-Ala-Aib-ψ(CSNH)-L-Ala-OMe, Ac-L-Ala-Aib-ψ(CSNH)-L-Ala-OMe, and Ac-ψ(CSNH)-L-Ala-Aib-L-Ala-OMe, determined by x-ray diffraction analyses, are reported. In all cases the peptide chain is folded with ϕ,ψ angles close to or slightly distorted from those expected for a type II β-bend conformation. However, the 4 → 1 H-bond distance falls within the accepted limits only for Ac-L-Ala-Aib-ψ(CSNH)-L-Ala-OMe. The structures are compared with those already published for their two oxygenated analogues.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bip.360270504
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