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  • Cell & Developmental Biology  (25,032)
  • Chemical Engineering  (17,982)
  • 1
    Keywords: Biomass conversion ; Biotechnology ; Chemical Engineering ; Chemistry industry ; Industrial Chemistry ; Kent ; Riegel ; biochemical engineering
    Description / Table of Contents: Substantially revising and updating the classic reference in the field, this handbook offers a valuable overview and myriad details on current chemical processes, products, and practices. No other source offers as much data on the chemistry, engineering, economics, and infrastructure of the industry. The Handbook serves a spectrum of individuals, from those who are directly involved in the chemical industry to others in related industries and activities. It provides not only the underlying science and technology for important industry sectors, but also broad coverage of critical supporting topics. Industrial processes and products can be much enhanced through observing the tenets and applying the methodologies found in chapters on Green Engineering and Chemistry (specifically, biomass conversion), Practical Catalysis, and Environmental Measurements; as well as expanded treatment of Safety, chemistry plant security, and Emergency Preparedness. Understanding these factors allows them to be part of the total process and helps achieve optimum results in, for example, process development, review, and modification. Important topics in the energy field, namely nuclear, coal, natural gas, and petroleum, are covered in individual chapters. Other new chapters include energy conversion, energy storage, emerging nanoscience and technology. Updated sections include more material on biomass conversion, as well as three chapters covering biotechnology topics, namely, Industrial Biotechnology, Industrial Enzymes, and Industrial Production of Therapeutic Proteins.
    Pages: Online-Ressource (XIV, 1562 pages)
    ISBN: 9780387278438
    Language: English
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  • 2
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    MDPI - Multidisciplinary Digital Publishing Institute
    Publication Date: 2023-06-23
    Description: The aim of this second Eng Special Issue is to collect experimental and theoretical re-search relating to engineering science and technology. The general topics of Eng are as follows: electrical, electronic and information engineering; chemical and materials engineering; energy engineering; mechanical and automotive engineering; industrial and manufacturing engineering; civil and structural engineering; aerospace engineering; biomedical engineering; geotechnical engineering and engineering geology; and ocean and environmental engineering. Therefore, the following editorial is a selection of representative works of these topics.
    Keywords: &nbsp ; Environment Management ; Environmental Engineering ; Chemical Engineering ; Materials Engineering&nbsp ; bic Book Industry Communication::T Technology, engineering, agriculture::TB Technology: general issues ; bic Book Industry Communication::T Technology, engineering, agriculture::TB Technology: general issues::TBX History of engineering & technology
    Language: English
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  • 3
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    De Gruyter | De Gruyter
    Publication Date: 2024-04-05
    Description: The essential principles of green chemistry are the use of renewable raw materials, highly efficient catalysts and green solvents linked with energy efficiency and process optimization in real-time. Experts from different fields show, how to examine all levels from the molecular elementary steps up to the design and operation of an entire plant for developing novel and efficient production processes.
    Keywords: Process Engineering ; Chemical Engineering ; Technical Chemistry ; thema EDItEUR::P Mathematics and Science::PN Chemistry ; thema EDItEUR::R Earth Sciences, Geography, Environment, Planning::RN The environment ; thema EDItEUR::R Earth Sciences, Geography, Environment, Planning::RN The environment::RNU Sustainability ; thema EDItEUR::T Technology, Engineering, Agriculture, Industrial processes::TD Industrial chemistry and manufacturing technologies::TDC Industrial chemistry and chemical engineering ; thema EDItEUR::T Technology, Engineering, Agriculture, Industrial processes::TG Mechanical engineering and materials::TGM Materials science ; thema EDItEUR::T Technology, Engineering, Agriculture, Industrial processes::TQ Environmental science, engineering and technology
    Language: English
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  • 4
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 2 (1982), S. 225-242 
    ISSN: 0886-1544
    Keywords: spermatozoa ; calcium ion transport ; motility regulation ; cholinergic agonists ; ouabain ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Behavioral responses of mature spermatozoa treated with neurotropic factors suggest that calcium entry and intracellular transport may be regulated by a cholinergic mediated program. To test the validity of this proposed mechanism, the effect of several agents on Ca distribution in the sperm cell was examined cytochemically.Sites of Ca accumulation were visualized in thin sections of bull spermatozoa by the application of a modification of Gomori's histochemical procedure for phosphatases. Intact bull sperm cells incubated at room temperature in a buffered balanced salt solution containing 5 mM/liter of CaCl2 showed small, randomly scattered deposits of the reaction product. Similarly treated sperm cells, plasmolyzed in hypoosmotic KCl, revealed a greatly increased amount of deposit associated with the cell membranes (mitochondrial surfaces and plasmalemma), the axonemal complex components, and satellite fibers adjacent to the outer dense fibers. Preincubation of intact cells in nicotine or eserine considerably enhanced the entry of calcium into the cell and its association with the membranes and other intracellular organelles. Decamethonium, an irreversible depolarizer and blocker of cholinergic receptors, interfered with the uptake and intracellular distribution of the calcium. Ouabain, the digitalis glycoside that decreases progressive motility of bull sperm and inhibits Na-, K-ATPase, appears to block Ca efflux, causing an intense accumulation of electron-opaque particles in the plasma membrane while smaller numbers of particles are distributed sparsely throughout the cell interior.The cytochemical results showing enhanced calcium entry in the presence of cholinergic agents, depressed intracellular calcium in cells treated with cholinergic receptor blocker, and intense accumulation of calcium within the cell membrane in the presence of ouabain are consistent with spermatozoan behavioral responses to these agents. These observations support the concept that neurotropic factors may be involved in regulating transmembrane and intracellular transport of ions in control of sperm cell function.
    Additional Material: 7 Ill.
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  • 5
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 2 (1982), S. 309-315 
    ISSN: 0886-1544
    Keywords: tropomyosin ; avian muscular dystrophy ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The isotype pattern of tropomyosin was investigated in normal and dystrophic avian pectroal muscle using two-dimensional gel electrophoresis. Previous reports have shown that adult pectoral muscle of chickens contains only the α-subunit of tropomyosin and a breast-type troponin-T (TN-T), whereas pectoral fetal muscle contains both α- and β-tropomyosin and leg-type TN-T. The change from the fetal to the adult forms begins shortly after hatching. It has been previously reported that avian dystrophic pectoral muscle contains both the leg- and breast-type TN-T; we show that in avian dystrophic muscle there is also persistent expression of the β-subunit of tropomyosin.
    Additional Material: 4 Ill.
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  • 6
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 2 (1982) 
    ISSN: 0886-1544
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 2 (1982), S. 287-308 
    ISSN: 0886-1544
    Keywords: actin-binding protein ; Dictyostelium ; cytoskeleton ; amoeboid movement ; calcium ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: A protein from Dictyostelium discoideum with an apparent subunit molecular weight of 95,000 daltons (95K protein) was previously identified as an actin-binding protein ‘Hellewell and Taylor, 1979’. In this paper, we present a method for purifying the protein, and characterize some important aspects of its structure and function. Purification of the 95K protein is achieved by fractionation with ammonium sulfate followed by chromatography on DEAE-cellulose, gel filtration on 6% agarose, and final purification on hydroxyapatite. The 95K protein is a dimer, composed of apparently identical subunits. It is a rod-shaped molecule, 38 nm in length, with a Stokes radius of 74 Å. In these structural properties, the 95K protein is similar to muscle and nonmuscle α-actinins. The 95K protein and filamin are equally competent, when compared on a weight basis, to enhance the apparent viscosity of actin as determined by falling ball viscometry. The apparent viscosity of mixtures of the 95K protein and actin is dramatically reduced at pH greater than 7.0 or free ‘Ca2+’ greater than 10-7 M. We also examine the mechanism by which calcium regulates the interaction of the 95K protein and actin. A change in free ‘Ca2+’ induces no detectable change in the quaternary structure of the 95K protein. Our experiments indicate that the 95K protein does not dramatically alter the length distribution of actin filaments in the presence of micromolar free ‘Ca2+’. A large fraction of the 95K protein cosediments with actin in the presence of low free ‘Ca2+’ (ca. 3 × 10-8M), but not in the presence of high free ‘Ca2+’ (ca. 4 × 10-6M). We conclude that increased free ‘Ca2+’ inhibits gelation of actin by the 95K protein by reducing the affinity of the 95K protein for actin. We propose that 95K protein is an important component of the cytoskeletal/contractile system in D. discoideum amoebae.
    Additional Material: 14 Ill.
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  • 8
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 2 (1982), S. 343-354 
    ISSN: 0886-1544
    Keywords: NBD-phallacidin ; actin ; ocular tissues ; wound repair ; stress fibers ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The fluorescent derivative of the actin-binding toxin phallacidin, 7-nitrobenz-2-oxa-1,3 diazole phallacidin, has been used to cytologically demonstrate the presence of actin in lens epithelium, corneal endothelium, and retinal pigment epithelium. In these noninjured tissues, no stress fibers are observed and fluorescence is confined mainly to an area at or near the cell membrane, although some diffuse cytoplasmic staining can also be seen. However, following injury to either the lens epithelium or corneal endothelium of rats and frogs, stress fibers are detected, but only in those cells that migrate into the wound area. Cells on the periphery of each tissue do not partake in would repair and thus maintain their normal appearance. After the tissue has regenerated, stress fibers disappear, and those cells involved in the injury response return to their normal morphology.When rabbit corneal endothelium is placed in tissue culture, stress fibers are observed as the cells migrate away from the initial explant. Upon reaching confluency, these cells spread out and each is surrounded by thick actin-containing bands. Furthermore, they exhibit some stress cables within their cytoplasm. This is in contrast to their appearance in vivo where stress fibers are absent and fluorescence is limited to a region near the cell membrane.
    Additional Material: 4 Ill.
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  • 9
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 2 (1982), S. 369-383 
    ISSN: 0886-1544
    Keywords: motility ; flagella ; cilia ; microtubules ; Gregarines ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The male gametes of the parasitic protozoan, Lecudina tuzetae, have a motile flagellum with a “6 + O” ultrastructure ‘Schrével and Besse, 1975’. These gametes were isolated from the cysts in which they develop and were observed and photographed under a variety of conditions. The flagella beat continuously, without stopping and starting, with a beat period of about 2 sec. They can beat in solutions whose viscosities are greater than 0.5 Nsm-2 (l Nsm-2 = 103 cP). The waveform can be approximated by a series of helical arcs and interconnecting straight regions that travel from the base to the tip. The helical regions have a radius of curvature of 3.2 μm and subtend a final angle of 1.7 radians. The straight portions are 2.0 μm in length. There are two sets of opposing bends, but they do not originate in the same plane. The resulting waveform is an approximately helical coil, with a pitch of 9.8 μm, a pitch angle of 0.6 radian and a peak-to-peak amplitude of 2.3 μm. The sense of the coil is left handed. The axoneme twists during beating. The main differences between the movement of this flagellum and that of typical 9 + 2 flagella are a low beat frequency and three-dimensional bends that produce relatively little forward movement of the cell. Twisting is discussed as a means of discriminating between some types of models of flagellar motility.
    Additional Material: 8 Ill.
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  • 10
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 2 (1982), S. 429-443 
    ISSN: 0886-1544
    Keywords: 21S dynein ; tubulin ; binding stoichiometry ; ATP sensitivity ; binding cooperativity ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The binding properties of Tetrahymena 21S dynein to doublet A and B subfiber microtubules were analyzed by both a turbidimetric assay (Δ A350 nm) and electron microscopy. KCl-extracted, sucrose-gradient, purified 21S dynein binds to each of the two kinds of axonemal microtubules in both ATP-insensitive and ATP-sensitive modes, even though only a single type of binding occurs to each of the subfibers in situ. Total dynein bound to axonemal microtubules is a composite of binding that is sensitive to dissociation by ATP and binding that is insensitive to ATP. Each exhibits a different binding profile. Total binding exhibits a sigmoid profile (h = 1.93) and saturates at 1.49 mg D/mg T. ATP-sensitive binding likewise exhibits a sigmoid profile (h = 2.66) but saturates at 1.06 mg D/mg T. Binding occurs with a similar affinity for both A and B subfibers. The Hill coefficient (h) for ATP-sensitive binding implies positive cooperativity between binding events. ATP-insensitive binding was studied independently in 20 μM ATP, 10 μM vanadate, which blocks ATP-sensitive binding. ATP-insensitive binding exhibits a hyperbolic profile (h = 1.0) and likewise occurs along each of the two kinds of axonemal tubules. Binding saturates at 0.87 mg D/mg T. The binding data suggest that the tubulin dimer has conserved both ATP-sensitive and ATP-insensitive binding sites for 21S dynein, even though the sites may not be expressed in vivo.
    Additional Material: 6 Ill.
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