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  • 1
    ISSN: 1432-1076
    Keywords: Hypophosphataemic rickets ; 1,25(OH)2D ; 1α-hydroxylase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract In 1974, a 2-year-old boy was diagnosed as having X-linked hypophosphataemic rickets (XLH) because of severe rickets and hypophosphataemia. The vitamin D metabolite concentrations, blood and urine chemistry and renal 25-hydroxyvitamin D3 (25 OHD3)-1α-hydroxlase were measured in 1982 (about 2 weeks after withdrawal of medication). 1α-hydroxylase was 392 pg/mg tissue/20 min in the patient, which was high compared with aged-matched controls (69.7±28.5 pg/mg tissue/20 min, mean ±SD, n=7). Our present studies showed that the 1α-hydroxylase activity in the patient with XLH was elevated. Therefore, the normal or low 1,25-dihydroxyvitamin D3 (1,25-(OH)2D3) concentrations in XLH patients could be due to accelerated catabolism of 1,25-(OH)2D3 or abnormally regulated 25OHD3-1α-hydroxylase in response to hypophosphataemia, although significantly elevated above that in normal controls.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1432-0568
    Keywords: Temporomandibular joint ; Immunohistochemistry ; Proteoglycan ; Aging ; Development
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract There is little information available regarding the morphological and biomolecular characteristics of mandibular condylar cartilage. The purpose of this study was to determine the age-related changes in the morphology and immunolocalization of glycosaminoglycans (GAGs) in mandibular condyles. The mandibular condylar cartilages from 4-, 8-, 16-, 32-, and 64-week-old Wistar male rats were examined to verify the localization of chondroitin-4-sulfate (Ch-4S), chondroitin-6-sulfate (Ch-6S) and keratan sulfate (KS) using an indirect immunofluorescent technique with three monoclonal antibodies for glycosaminoglycans, 2-B-6, 3-B-3 and 5-D-4, respectively. Morphologically, the condylar cartilage was a growth cartilage during growing periods, began to differentiate into articular cartilage from the central area of 16-week-old condyles, and became mature articular cartilage at 32 weeks of age. A regional difference was found in the morphological features and distribution of GAGs between the anterior, central, postero-superior and posterior areas of the condyles at each age. The immunohistochemical localizations of these three glycosaminoglycans showed age-related, morphology-dependent changes, from growth cartilage to articular cartilage-like cartilage. Immunoreactions for all of the antibodies decreased progressively with age in the interterritorial matrix, while the pericellular and territorial matrix in the condylar cartilage of the mandible maintained relatively higher immunoreactivity. In conclusion, age-related and regional differences in the localization of glycosaminoglycans Ch-4S, Ch-6S, and KS were found in the mandibular condyles in rats, and these changes are believed to be related to functional and developmental requirements.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    World journal of microbiology and biotechnology 13 (1997), S. 355-356 
    ISSN: 1573-0972
    Keywords: Achlorophyllous alga ; enzymatic degradation ; protoplast formation ; Prototheca.
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract The effects of experimental factors on protoplast formation of Prototheca zopfii Kru¨ger in 0.85 m NaCl using Macerozyme R-200 were studied based on a fractional factorial experimental design. The rate of protoplast formation was mainly affected by the incubation temperature and the age of algal cells. The optimal condition for the maximum protoplast yield was determined based on a response surface model. These were: mid-logarithmic phase cells and Macerozyme concentration of 4% at a temperature of 35°C.
    Type of Medium: Electronic Resource
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