Library

feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
Filter
  • 1990-1994  (3)
  • 1960-1964
  • 1992  (3)
Material
Years
  • 1990-1994  (3)
  • 1960-1964
Year
  • 1
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of periodontal research 27 (1992), S. 0 
    ISSN: 1600-0765
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Phospholipase A2 (PLA2) is a proinflammatory enzyme in the synovial fluids of all - and sera of some - patients with rheumatoid arthritis. Due to the similarities in pathogenesis between rheumatoid arthritis and periodontitis, we sought to study the enzymatic properties of PLA2 in periodontal tissue. In this study, we demonstrated PLA2 activity in rat gingival tissue, about 80% of which was present in the cytosolic fraction. We characterized the cytosolic PLA2 enzyme with respect to substrate specificity, sensitivity to detergent, Ca2+ ion dependency and optimum pH. We found that phosphatidylethanolamine, rather than phosphatidylcholine, was the preferred substrate, the Ca2+ ion was essential for the expression of PLA2 activity, the enzyme was active over a broad pH range, with the optimum at pH 9.0, and sodium-deoxycholate inhibited the enzyme activity strongly in a concentration-dependent manner. These results are consistent with those which have been obtained with synovial fluid PLA2 and suggest that gingival PLA2 may be involved in the pathogenic processes of gingivitis and periodontitis.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Entomologia experimentalis et applicata 63 (1992), S. 273-281 
    ISSN: 1570-7458
    Keywords: Diapause ; photoperiod ; rice stem maggot ; Chlorops oryzae ; Chloropidae
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Chlorops oryzae is bivoltine in northern Japan but trivoltine in the southern part of the country. In the bivoltine strain, both the egg and larval stages were found to be sensitive to photoperiod. When the egg stage was exposed to a long-day photoperiod (16L:8D), larval development showed a short-day type response, and mature third-instar larvae entered a summer diapause under a long-day photoperiod (15L:9D). When eggs experienced short days, the first-instar larvae entered a winter diapause under short-day conditions, and the critical photoperiod in the larval stage ranged from about 14L:10D to about 12L:12D as the photoperiod experienced by the eggs increased from 12L:12D to 14L:10D. However, the development of the larvae after overwintering was not influenced by the photoperiod. In the trivoltine strain, larval development was retarded under a 14L:10D photoperiod but not under either shorter or longer photoperiods, when larvae had spent the egg stage under a 16L:8D photoperiod. The critical photoperiod of the larval stage for the induction of a winter diapause in the first instar was about 12L:12D, though it varied to some extent with the photoperiod during the egg stage. Thus, Chlorops oryzae was able to adapt itself to the local climatic conditions by the development of variable and complicated photoperiodic responses.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 3
    ISSN: 1615-6102
    Keywords: Actin ; Actomyosin ; In vitro Motility assay ; Myosin ; Pollen tube
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Myosin in pollen tubes ofLilium longiflorum was partially purified, using an in vitro motility assay as a monitor. The main components in the partially purified preparation had molecular masses of 110, 120, and 140 kDa in SDS-PAGE. They became bound to actin filaments in an ATP-dependent manner. Among the components, only that of 120 kDa became bound to ATP and was concluded to be the heavy chain of pollen tube myosin.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...