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  • Cell & Developmental Biology  (89)
  • Biochemistry and Biotechnology  (49)
  • 13C NMR  (10)
  • 1
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: A procedure for the isolation of protein markers of epidermal differentiation in vitro is described. Human epidermal keratinocytes were cultured and radiolabelled in vitro. Fractionation was performed according to buoyant density (which reflects the degree of terminal differentiation) using Percoll density gradient centrifugation. Subpopulations of keratinocytes were characterised using light and electron microscopy, and proteins fractionated using high resolution two-dimensional gel electrophoresis. Radio-labelled proteins were detected using autoradiography and fluorography. Integral membrane proteins were characterised using Triton X-114 phase shift extraction. Data from this in vitro study were compared to silver stained gels of samples from intact epidermis (in vivo). We report quantitative differences between 14 specific protein moieties expressed in subpopulations of keratinocytes and identify some of these proteins. The differential expression of these protein markers and their possible use in the interpretation of the keratinocyte maturation pathway in cultured cells from patients with skin diseases are discussed.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: A procedure is described for the detection of keratinocyte specific proteins. Fibroblasts and keratinocytes were isolated from human skin and radiolabelled in vitro. Samples were separated by two-dimensional polyacrylamide gel electrophoresis to compare the proteins synthesised by the different types of cultured skin cells. Dual label autoradiography of samples radiolabelled with [35S]methionine and [75Se]selenomethionine was used to identify keratinocyte specific proteins. We report 45 keratinocyte-specific components and identify some of these proteins. The differential expression of these proteins and their relevance to epidermal differentiation are discussed.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Weinheim : Wiley-Blackwell
    Electrophoresis 12 (1991), S. 579-584 
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Using histochemical techniques an abnormal programme of epidermal differentiation has been well documented in psoriasis. In order to characterise further the biochemistry of this process we have cultured dermal fibroblasts and epidermal keratinocytes from involved psoriatic skin. This has facilitated metabolic radiolabelling of skin cells and analysis of protein synthesis by two-dimensional polyacrylamide gel electrophoresis. The expression of keratin and differentiation markers was identical to that of normal keratinocytes, suggesting that psoriatic epidermal differentiation is not truncated in vitro as has been postulated to be the case in vivo. Low molecular mass components (5-8.5 kDa), previously shown to be upregulated in suprabasal keratinocytes, were detected in epidermal fractions from psoriatic skin enriched for basal cells. Of especial interest was a component of 26 kDa, pI 5.9, which was highly upregulated in psoriatic as compared to normal cultured keratinocytes and was not detected in fibroblasts. These findings are in accord with a qualitatively abnormal pattern of differentiation for keratinocytes in the involved psoriatic epidermis.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Journal of Morphology 166 (1980), S. 337-386 
    ISSN: 0362-2525
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Three categories of dietary adaptation are recognized - faunivory, frugivory, and folivory - according to the distinctive structural and biochemical features of animal matter, fruit, and leaves respectively, and the predominance of only one in the diets of most species.Mammals subsisting mainly on animal matter have a simple stomach and colon and a long small intestine, whereas folivorous species have a complex stomach and/or an enlarged caecum and colon; mammals eating mostly fruit have an intermediate morphology, according to the nature of the fruit and their tendency to supplement this diet with either animal matter or leaves. The frugivorous group are mostly primates: 50 of the 78 mammalian species, and 117 of the 180 individuals included in this analysis are primates.Coefficients of gut differentiation, the ratio of stomach and large intestine to small intestine (by area, weight, and volume), are low in faunivores and high in folivores; the continuous spread of coefficients reflects the different degrees of adaptation to these two dietary extremes.Interspecific comparisons are developed by allowing for allometric factors. In faunivores, in which fermentation is minimal, the volume of stomach and large intestine is related to actual body size, whereas these chambers are more voluminous in larger frugivores and mid-gut fermenting folivores; fore-gut fermenters show a marked decrease in capacity with increasing body size. Surface areas for absorption are related to metabolic body size, directly so in frugivores; area for absorption is relatively less in larger faunivores and more in larger folivores, especially those with large stomachs.Indices of gut specialization are derived from these regressions by nonlinear transformation, with references to the main functional features of capacity for fermentation and surface area for absorption.These are directly comparable with the dietary index, derived from quantitative feeding data displayed on a three-dimensional graph, with all species within a crescentic path from 100% faunivory through 557ndash;80% frugivory to 100% folivory, perhaps illustrating, at least for primates, the evolutionary path from primitive insectivorous forms through three major ecological grades.
    Additional Material: 29 Ill.
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  • 5
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 51 (1996), S. 375-383 
    ISSN: 0006-3592
    Keywords: cellulase ; enzyme recycling ; enzyme adsorption ; lignocellulosic hydrolysis ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Past technoeconomic modeling work has identified the relatively large contribution that enzymatic hydrolysis adds to the total cost of producing ethanol from lignocellulosic substrates. This cost was primarily due to the high concentration of enzyme and long incubation time that was required to obtain complete hydrolysis. Although enzyme and substrate concentration and end-product inhibition influenced the rate of hydrolysis, the effect was less pronounced during the initial stages of hydrolysis. During this time most of the cellulases were adsorbed onto the unhydrolyzed residue. By recycling the cellulases adsorbed to the residual substrate remaining after an initial 24 h, a high rate of hydrolysis, with low overall residence time and minimal cellulase input, could be achieved for several rounds of enzyme recycle. A comparison of the front end (pretreatment, fractionation, and hydrolysis) of a softwood/hardwood to ethanol process indicated that the lignin associated with the softwood-derived cellulose stream limited the number of times the cellulose containing residue could be recycled. © 1996 John Wiley & Sons, Inc.
    Additional Material: 7 Ill.
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  • 6
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 2 (1982), S. 9-24 
    ISSN: 0886-1544
    Keywords: amoebae ; actinopoda ; heliozoa ; Actinophrys ; phagocytosis ; pseudopodia ; membrane ; extrusomes ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Two phases of prey capture by the heliozoon Actinophrys sol are documented by electron microscopy. The phases are those of prey adhesion to the predator and enclosure of the prey by the predator. Adherence is brought about by numerous small pieces of adhesive membrane produced by the predator at the site of prey contact. Some of the heliozoan extrusomes expel their contents at this time, but the significance of this event is unclear. Enclosure of the prey is effected by a funnelshaped pseudopodium. This is drawn over the prey by the action of the leading margin. The ultrastructural appearance of the cytoplasm of the leading margin differs from the rest of the cell, being homogeneous and finely filamentous. Both force and traction for the progression of the pseudopod are generated primarily at the tip. During the development of the funnel-pseudopod, extrusomes expand and fuse with each other and with the plasma membrane. Their investing membrane is thereby made available as food vacuole membrane.
    Additional Material: 9 Ill.
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  • 7
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 2 (1982), S. 599-614 
    ISSN: 0886-1544
    Keywords: monoclonal antibodies to tubulin ; radioimmune assay ; immunoautoradiography ; Western blots ; immunofluorescence ; tubulin heterogeneity ; eukaryotic flagellar motility ; immunomotility ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Two monoclonal antibodies reactive for α-tubulin but not for β-tubulin have been prepared, characterized in terms of their relative binding to tubulins from differnt sources by a solid-phase binding assay, immunoautoradiography, and indirect immunofluorescence, and utilized to study flagellar motility. Our results demonstrate that α-tubulins from different species, and even from different tissues of the same species, are nonidentical. Especially interesting was the observation that one of the antibodies, Ab2, immunofluorescently stained microtubules of chick embryo fibroblast cells, but was completely unreactive for microtubules of rat kangaroo (PtK2) fibroblasts; a different antibody, Ab1, stained both cell types. Results of these and additional experiments clearly show that Ab1 and Ab2 recognize discrete and different epitopes on α-tubulin.Monoclonal antitubulins Ab1 and Ab2 each inhibited the bend amplitude of reactivated sea urchin spermatozoa without affecting beat frequencies or the ability of the outer doublet microtubules to slide past each other in elastase-digested models. These results, together with those obtained previously using rabbit polyclonal antitubulin antibodies [Asai and Brokaw, 1980], demonstrate that inhibition of bend amplitude is a common property of antitubulin antibodies and is not due to the binding of antibodies to one specific site on the axoneme. Our results suggest that tubulin subunit conformational changes may occur on the outer doublet lattice and may be integrally involved in the mechanism and control of flagellar bending.
    Additional Material: 5 Ill.
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  • 8
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 14 (1989), S. 21-25 
    ISSN: 0886-1544
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Additional Material: 1 Ill.
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  • 9
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 18 (1991), S. 204-214 
    ISSN: 0886-1544
    Keywords: actin-binding ; muscle ; Z-line ; capping ; isoform ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Chicken adult muscle and liver cDNA libraries were screened with a cDNA, α1, previously isolated from a chicken embryo library by screening with antibodies against the α subunit of chicken CapZ. cDNAs with a new coding region, called α2, were found in addition to ones with the α1 coding region. α2 predicts a protein sequence that matches exactly the N-terminal sequence of 5 peptides prepared from CapZ α purified from chicken muscle, while the protein sequence predicted by α1 matches the peptides well, but not exactly. The predicted protein sequences of α1 and α2 are very similar to each other, and they are similar to those of the α subunit of capping protein from Dictyostelium [Hartmann et al., J. Biol. Chem. 163:5254-5254, 1989] and an actin-binding protein from Xenopus [Ankenbauer et al., Nature 342:822-824, 1989]. Other conserved features of the predicted primary and secondary structures are noted. Chicken α1 and α2 are transcribed in all of 7 adult chicken muscle and non-muscle tissues in comparable amounts by Northern analysis. α2 has four poly(A)+ RNA transcripts, one of which is rare in liver. α1 has two transcripts. α1 and α2 are encoded by different single-copy genes by Southern analysis of chicken genomic DNA.
    Additional Material: 7 Ill.
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  • 10
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 32 (1995), S. 129-132 
    ISSN: 0886-1544
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
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