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  • Wiley-Blackwell  (61)
  • Milton :Taylor & Francis Group,  (1)
  • 1990-1994  (62)
  • 1935-1939
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Language
Years
Year
  • 1
    Online Resource
    Online Resource
    Milton :Taylor & Francis Group,
    Keywords: Royal Institution od Great Britain-History. ; Electronic books.
    Description / Table of Contents: Michael Faraday's life and his relationship with the Royal Institution speak to us across the years, making for a fascinating read. Written in a concise, nontechnical style, Michael Faraday and the Royal Institution: The Genius of Man and Place is a human account that provides an introduction to the roots of modern science and ways in which scientists work. The book is lavishly illustrated with drawings, cartoons, photographs, and letters-many never before published. There is no similar book on Faraday that interprets his genius in modern, everyday terms, making it understandable, interesting, and exciting reading for scientists and nonscientists alike.
    Type of Medium: Online Resource
    Pages: 1 online resource (247 pages)
    Edition: 1st ed.
    ISBN: 9781482229493
    DDC: 509.2
    Language: English
    Note: Cover -- Half Title -- Title Page -- Copyright Page -- Dedication -- Contents -- Foreword -- Preface Michael Faraday and The Royal Institution -- Chapter 1: Setting the Scene -- Chapter 2: Rumford, Davy and The Royal Institution -- Chapter 3: From Errand Boy to the Grand Tour -- Chapter 4: Faraday's Scientific Contributions -- Chapter 5: Faraday's Writings -- Chapter 6: Faraday the Man -- Chapter 7: Faraday's Influence upon The Royal Institution -- Chapter 8: The Popularization of Science -- Epilogue -- Appendix V: Part of The Royal Institution Lecture Calendar, 1933 -- Appendix IV: Discourses Arranged by Faraday (before 1862) -- Appendix III: Faraday's Friday Evening Discourses,1835 onwards -- Appendix II: Learned Societies to which Faraday was Elected -- Appendix I: Faraday's Discourses & -- Scientific Publications, 1832-1834 -- Index.
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  • 2
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The signal sequence of a nuclear-directed protein encodes the necessary information for targeting the attached proteins to the cell nucleus. The sequence/structural requirements for a functional transport signal were explored with a series of peptides derived from the simian virus 40 large T-antigen nuclear signal 126-134 (CPKKKRKVED-NH2, wild type) conjugated to bovine serum albumin (BSA) through an N-terminal Cys (1) with m-maleimidobenzoyl-N-hydroxysuccinimide ester. Nuclear accumulation was virtually complete 15 min after microinjection into green monkey kidney cells (TC-7). Peptides with Asn, Orn, and Gln substituted for Lys128, the reverse wild-type peptide (DEVKRKKKPC-NH2) and the long 34-residue wild-type analogue (CYDDEATADSQHSTPPKKKRKVEDPKDFESELLS-NH2), were synthesized and conjugated similarly to BSA. The Orn peptide and the 34-residue wild-type analogue conjugated to BSA also transported to the nucleus but at a slower rate than 1. The reverse wild-type, Asn- and Gln-BSA conjugates of these signal analogues did not show transport to the nucleus after 6 h of incubation. In an effort to learn if such signal sequences would also target a small molecule such as a fluorescent tag to the nucleus, 1 fluorescently tagged with monobromobimane was prepared and microinjected into TC-7 cells. The peptide was distributed throughout the cell. These results support the notion that a positively charged residue at position 128 is needed for rapid nuclear transport and that the intracellular transport machinery has spatial recognition. The results with fluorophore-peptide conjugates suggest nuclear localization of these low molecular weight peptides will be difficult to attain even if attached to a functional nuclear localization sequence.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Biomedical Chromatography 4 (1990), S. 148-151 
    ISSN: 0269-3879
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: High performance liquid chromatography (HPLC) with a TSK-4000SW gel filtration column was used to compare envelope polypeptides from four strains of herpes simplex virus type 1 (HSV-1). The chromatographic profiles demonstrated polypeptide variability among three clinical strains and the wild-type F strain. Radioimmunoprecipitation of the HPLC fractions with polyclonal anti-HSV-1 followed by SDS-polyacrylamide gel electrophoresis (PAGE) of the immunoprecipitates revealed molecular weight differences of various polypeptides in fractions from the area containing major peaks. This HPLC method could prove useful for the analysis of polypeptide polymorphism in clinical isolates of HSV-1, as well as in other viruses.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Journal of Chemometrics 5 (1991), S. 417-434 
    ISSN: 0886-9383
    Keywords: Factor analysis ; Power density distribution ; Chromatography ; Absorption spectroscopy ; Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Evaluation of the results of factor analysis of sets of spectroscopically detected chromatograms is carried out by examining the shapes of the abstract factors. This is done either by visual inspection or by analysis of the power density spectra produced from them. Owing to constraints imposed by the column function and the spectroscopic instrument function, the information content of the chromatograms necessarily occurs at low spatial frequencies. As a consequence, it appears as relatively broad features in the abstract chromatograms and as a peak in the low-frequency region of the corresponding power density plot. On the basis of examination of the power density distribution, a well-defined distinction is made between primary and secondary abstract factors. The major uncertainty encountered in determining the number of chemical components appears to arise from effects of contaminants in reagents.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
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  • 5
    ISSN: 0886-1544
    Keywords: organelle translocation ; translocator ; actin-dependent ATPase ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The dispersion of carotenoid droplets in permeabilized goldfish xanthophores is dependent on ATP, F-actin, and cytosol. We report here that the motor (ATPase, translocator) resides with the permeabilized cell remnants and not in the cytosol. We also report that the carotenoid droplets have an ATPase that is not conventional myosin, dynein, or an ion pump. Its activity appears to correlate with the actin content of the carotenoid droplet preparation. A carotenoid droplet protein of Mr 72,000 (p72) is shown to be labeled by irradiation with 8-azido-ATP with concomitant loss of ATPase activity of the carotenoid droplets. We propose that this protein may be the ATPase responsible for carotenoid droplet dispersion.
    Additional Material: 9 Ill.
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 25 (1993), S. 358-368 
    ISSN: 0886-1544
    Keywords: smooth muscle ; smooth muscle myosin ; nonmuscle myosin ; myosin isoforms ; cellular myosin ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: In smooth muscle tissue, two or three isoforms of myosin heavy chain (MHC) have been reported (SM1, SM2, and/or NM). In mouse uterus tissue, four bands in the region of the MHC's can be resolved on high resolution SDS polyacrylamide gels. Western blots using smooth muscle (SM) MHC-specific and nonmuscle (NM) MHC-specific polyclonal antibodies show the upper two bands in the MHC region are SM isoforms, whereas the lower two bands are NM isoforms. One-dimensional peptide maps of these four bands show each to have a unique pattern of polypeptide fragments following α-chymotrypsin digestion. Developmental expression of myosin heavy chains (MHC) in mouse uterus, aorta, bladder, and stomach (6 ages, 10-150 days) was determined using tissue homogenates. In the uterus, both SM MHC's show an increase in relative content with increasing age, whereas the NM MHC's show a decrease. The mouse aorta shows a significant increase in the SM MHC's and a significant decrease in the NM MHC from day 10 to day 30, which is similar to data reported for the rat aorta. Whereas both the bladder and stomach contain relatively small amounts of NM MHC's (∼ 10% or less), these quantities do show decreases with development. The SM1:SM2 ratio for the uterus remains high (3.4 at 150 days) through development; the aorta, bladder, and stomach also start out high, but tend toward 1.0 in the 150-day animals. The presence of four MHC isoforms in the uterus with unique developmental regulation of expression is consistent with hypotheses of unique functional roles for these isoforms. © 1993 Wiley-Liss, Inc.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 11 (1991), S. 158-158 
    ISSN: 0887-3585
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    Bognor Regis [u.a.] : Wiley-Blackwell
    Journal of Polymer Science Part A: Polymer Chemistry 28 (1990), S. 955-965 
    ISSN: 0887-624X
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: An extremely efficient process has been developed for the synthesis of linear silylene-acetylene and disilylene-acetylene polymers. Trichloroethylene is quantitatively converted by n-butyllithium to dilithioacetylene. Quenching with dialkyl-or diaryldichlorosilanes affords high yields of the polymers, \documentclass{article}\pagestyle{empty}\begin{document}$ \rlap{--} [{\rm SiR}_{\rm 2} \hbox{---} {\rm C} \equiv {\rm C\rlap{--} ]}_n ,{\rm and }\rlap{--} [{\rm SiMe}_{\rm 2} {\rm SiMe}_{\rm 2} - {\rm C} \equiv {\rm C\rlap{--} ]}_n $\end{document} if ClMe2SiSiMe2Cl is employed. Molecular weights are much higher with this route than when acetylene is used as the dilithio- or dimagnesium acetylide precursor. Some of these polymers can be pulled into continuous fibers, and all can be cast into coherent films and thermally converted into silicon carbide.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
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  • 9
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 39 (1992), S. 732-740 
    ISSN: 0006-3592
    Keywords: cell disruption ; chemical permeabilization ; Escherichia coli ; fermentation ; protein recovery ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Overall protein release greater than 75% in less than 1 h can be attained by exposing exponentially growing Escherichia coli cells to 0.4 M guanidine plus 0.5% Triton X-100 at 37°C in medium. Cell growth stops immediately upon addition of the chemicals, but the cells are not lysed. Guanidine concentrations lower than 0.2 M, in conjunction with 0.5% Triton X-100, do not release significant intracellular protein, nor do they inhibit cell growth. Under these conditions, the cells undergo an adaptation that confers resistance to protein release by further treatment with guanidine and Triton X-100. Cells treated with 0.2 M guanidine plus 0.5% Triton X-100 display intermediate behavior. Protein release is approximately 35%, and growth is temporarily interrupted by an extended lag phase. Subsequent resumption of cell growth results in resistant cells and no additional protein release. This resistance is shown to be reversible and is most likely due to physiological adaptation rather than genetic mutation.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
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  • 10
    Electronic Resource
    Electronic Resource
    Hoboken, NJ : Wiley-Blackwell
    AIChE Journal 37 (1991), S. 1529-1536 
    ISSN: 0001-1541
    Keywords: Chemistry ; Chemical Engineering
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Studies of the motion of a dilute suspension of 100-micron glass and stainless steel spheres in water flowing turbulently down a pipe revealed that they could be trapped in necklace formations that move slowly at a distance of less than one particle diameter from the wall. The tendency toward trapping increases with particle density and decreases with flow rate. The phenomenon is interpreted as occurring when the Saffman lift force toward the wall overcomes the ability of fluid turbulence to mix the particles. The location of the particles is dictated by a balance between the Saffman lift force and a wall-induced force associated with the displacement of fluid as a particle moves parallel to the wall.
    Additional Material: 11 Ill.
    Type of Medium: Electronic Resource
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