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  • 1
    ISSN: 1432-1793
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract We have monitored the incorporation of 3H-glycine into, and the excretion of, soluble tissue and extrapallial fluid proteins in the hardshell clam Mercenaria mercenaria in an attempt to follow some of the metabolic events that occur antecedent to shell deposition. After incubating at 20°C for 48 h, clams were killed and the distribution of incorporated and unincorporated tritium in seawater, mantle fluid, hemocoelic-tissue fluid, extrapallial fluid and tissue was determined. Most of the incorporated tritium was in the insoluble tissue proteins. Much more incorporated tritium was found in the hemocoelic-tissue fluid fraction than in the extrapallial fluid. We assume that most of the radioactivity we followed was due to free or incorporated radioactive glycine. The ratio of 3H-protein to 3H-glycine was greater in the extrapallial fluid than in the hemocoelic-tissue fluid, suggesting either protein secretion into or glycine removal from the extrapallium. We also observed that both 3H-protein and 3H-glycine concentrations were higher in the mantle fluid than in the external sea water, although the ratios of 3H-glycine to 3H-protein in these two fluids were not different.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1432-1793
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Sheets of mantle tissue from above the mantle line of Mercenaria mercenaria were incubated for 2, 6 and 20 h at 20°C in 50 μCi 3H-glycine in 50 ml artificial seawater. Incorporation of tritium into soluble proteins excreted by the mantle and into tissue proteins was followed. The excretion of soluble protein continued throughout the experiment; the proportion of incorporated label excreted reached 17% by 20 h. The initiation of excretion of labelled protein seemed to lag 60 to 70 min behind the initiation of protein synthesis. Protein synthesis by the mantle contributed to proteins of the extrapallium and mantle chambers and, thus, may be involved in synthesis and regulation of proteins involved in the shell-formation process.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Calcified tissue international 34 (1982), S. 211-213 
    ISSN: 1432-0827
    Keywords: Rat ; incisor ; ameloblasts ; enamel ; 45Ca autoradiography
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Summary Rats were injected with45Ca and horseradish peroxidase to determine the patterns of45Ca incorporation into incisor enamel and the morphological types of the overlying maturation ameloblasts.45Ca autoradiography showed no differences in the patterns of incorporation into enamel between routinely embedded and freeze-dried specimens. Enamel overlaid by ruffle-ended ameloblasts was much more heavily labeled while that overlaid by smooth-ended ameloblasts showed only moderate labeling. The observations lend further support to the hypothesis that the ruffle-ended cells are very active in mineralizing enamel and that the smooth-ended cells are in a passive, restorative phase.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Cell & tissue research 243 (1986), S. 91-99 
    ISSN: 1432-0878
    Keywords: Teeth ; Calcification ; Adenosine triphosphatase ; Calcium-alkaline phosphatase ; Rat
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Enzymatic activities of calcium-magnesium dependent adenosine triphosphatase (Ca-ATPase) and nonspecific alkaline phosphatase (ALPase) were localized at the initial calcification sites of dentin and enamel of rat incisor teeth using electron-microscopic cytochemistry. Ca-ATPase was localized in the Golgi cisternae, cytoplasmic vesicles and along the outer surface of the presecretory and secretory ameloblasts, whereas it was totally absent from the odontoblasts in the pulp. Inversely, ALPase reaction was localized along the outer surface of the odontoblasts, but almost completely absent from the ameloblasts. Diffuse extracellular reactions of both enzymes were distributed throughout the unmineralized fibrous matrix of mantle dentin in which a large number of matrix vesicles were scattered. Both Ca-ATPase and ALPase reactions, which appeared in the matrix vesicles in the process of formation of mantle dentin, became most conspicuous at the site of initial dentin calcification. At this stage, an intense Ca-ATPase reaction also appeared along some of the collagen fibrils adjacent to the reactive matrix vesicles. No ALPase reaction was localized along these Ca-ATPase reactive collagen fibrils. Our observations suggest strongly that Ca-ATPase in the matrix vesicles originates from the inner enamel epithelium and/or preameloblasts whereas ALPase originates from the odontoblasts in the pulp. The importance of the coexistence of both enzymes for the control of initial calcification of dental hard tissues is suggested.
    Type of Medium: Electronic Resource
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