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  • ELISA  (2)
  • Porcine secretory enamel  (2)
  • (+)-pinoresinol  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Endogenous pine wood nematicidal substances in pines, Pinus massoniana, P. strobus and P. palustris
    Amsterdam : Elsevier
    Phytochemistry 33 (1993), S. 1395-1401 
    Details
    ISSN: 0031-9422
    Keywords: (+)-pinoresinol ; (-)-nortrachelogenin ; P. palustris ; P. strobus ; Pinaceae ; Pinus massoniana ; bark ; heartwood ; methyl ferulate ; nematicides ; pinosylvin monomethylether ; repellents ; structure-activity relationship. ; α-humulene
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0031-9422(93)85098-C
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    The localization and characterization of proteinases for the initial cleavage of porcine amelogenin (1992)
    Springer
    Calcified tissue international 51 (1992), S. 213-217 
    Details
    ISSN: 1432-0827
    Keywords: Porcine secretory enamel ; Degradation of amelogenin ; Proteinases ; 25kDa amelogenin ; Enzymography
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Summary In the outermost layer of porcine-developing enamel adjacent to the ameloblasts in the secretory stage, the activities of two proteinases having molecular masses of 76 and 78kDa were detected by enzymography using gelatin as a substrate. On the other hand, high activities of known 30 and 34kDa proteinases were localized in the inner layer of the enamel. The 76kDa proteinase cleaved the carboxylterminal peptide of porcine 25kDa amelogenin to convert it to 20kDa amelogenin. The 78kDa proteinase also acted on the 25kDa amelogenin similarly, but its activity was weak. The results indicate that the 25kDa amelogenin synthesized and secreted by ameloblasts is converted to 20kDa amelogenin by the action of proteinase localized in the outermost layer of the secretory enamel, and then further degraded by the proteinases in the inner layer of the enamel associated with the increase of mineralization.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00334549
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Porcine amelogenins (1994)
    Springer
    Calcified tissue international 54 (1994), S. 69-75 
    Details
    ISSN: 1432-0827
    Keywords: Porcine secretory enamel ; Porcine amelogenin ; Plasma desorption mass spectometry ; Amino acid sequence ; CNBr cleavage
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Abstract Amelogenins were extracted from the thin outer layer of porcine secretory enamel and purified by gel filtration and reverse-phase HPLC. The results of amino acid sequencing of the purified porcine amelogenins indicated the presence of at least four prototype amelogenins translated from alternatively spliced transcripts. The results of mass spectroscopy of the CNBr-cleaved peptides derived from the 25kDa amelogenin indicated that porcine 25kDa amelogenin is neither phosphorylated nor glycosylated.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00316293
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    Paper (German National Licenses)
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  • 4
    Electronic Resource
    Electronic Resource
    Immunological determination of faecal haemoglobin concentrations in dogs (1998)
    Springer
    Veterinary research communications 22 (1998), S. 193-201 
    Details
    ISSN: 1573-7446
    Keywords: diagnosis ; dog ; ELISA ; faeces ; latex agglutination ; occult blood ; serology
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Faecal haemoglobin (Hb) concentrations in apparently healthy experimental Beagle dogs and in dogs of various breeds kept in private households or at breeders were measured by reversed passive latex agglutination (RPLA) and enzyme-linked immunosorbent assay (ELISA) in an effort to define the physiological concentrations of faecal Hb in the dog. In 88% (53) of 60 experimental Beagle dogs (30 males and 30 females), the RPLA titres were 1:2 and 1:8 and the faecal Hb concentrations ranged from 40.0 to 431.5 (mean 184.1±92.6) μg/g faeces by ELISA. No significant difference was found in Hb levels or RPLA titres between males and females. Seven dogs (12%) had significantly greater RPLA titres and Hb concentrations by ELISA than the remaining dogs. In 84% (45) of the 53 dogs kept in private households or at breeders, the RPLA titres were 〉1:1 to 1:8 and the faecal Hb concentrations ranged from 7.1 to 456.7 (mean 137.5±128.7) μg/g faeces in ELISA. Eight of these dogs (15.1% of 53 dogs) had significantly greater RPLA titres and Hb concentrations by ELISA than the remaining dogs. There were no significant differences between the Beagles and dogs kept in private households or at breeders. In conclusion, in 98 (86.7% of 113) dogs the physiological concentrations of RPLA titres were 〉1:1 to 1:8 and the faecal Hb concentrations were 143.5–185.1 μg/g (95% confidence level). Approximately 13.3% of apparently healthy dogs had higher faecal Hb concentrations, suggesting the presence of subclinical haemorrhages. Four dogs suffering from colorectal cancer also had high faecal Hb concentrations.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1006025422317
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  • 5
    Electronic Resource
    Electronic Resource
    Physiological levels of C-reactive protein in normal canine sera (1998)
    Springer
    Veterinary research communications 22 (1998), S. 77-85 
    Details
    ISSN: 1573-7446
    Keywords: C-reactive protein ; circadian rhythm ; dog ; ELISA ; physiological variation ; serum
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract This study was undertaken to investigate whether the level of C-reactive protein (CRP) in the serum of dogs undergoes physiological variation, using 10 normal Beagle dogs (5 males and 5 females), 1–2 years old, maintained in a healthy condition in a controlled environment. The CRP concentration in the sera collected seven times each day at intervals of approximately 3 h ranged from 0.8 to 16.4 µg/ml (mean 5.06±3.60) in one experiment and from 0.8 to 14.0 µg/ml (mean 4.50±2.80) in a second experiment. On examining the 24-h variations in the concentration of CRP in serum, neither consistent changes nor a definite pattern of circadian rhythm was detected. During 28 days observation, only very slight changes, which seemed attributable to analytical errors, were seen in any of the dogs, except one. The concentration of CRP in the serum during the 28 days ranged from 0.8 to 22.6 µg/ml (mean 3.65±1.40). The concentrations underwent no significant variations in individual dogs, but significant differences were found between the dogs (p〈0.01).
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1006071211779
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    Paper (German National Licenses)
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