Library

X
feed icon rss

Your email was sent successfully. Check your inbox.

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

Proceed reservation?

Export
  • 1
    Electronic Resource
    Electronic Resource
    A fluorescent probe and a photoaffinity labeling reagent to study the binding site of maytansine and rhizoxin on tubulin (1993)
    s.l. : American Chemical Society
    Bioconjugate chemistry 4 (1993), S. 284-289 
    Details
    ISSN: 1520-4812
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bc00022a006
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    Identification of Cellular Compartments Involved in Processing of Cathepsin E in Primary Cultures of Rat Microglia (1998)
    Oxford, UK : Blackwell Science Ltd
    Journal of neurochemistry 70 (1998), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: Cathepsin E is a major nonlysosomal, intracellular aspartic proteinase that localizes in various cellular compartments such as the plasma membrane, endosome-like organelles, and the endoplasmic reticulum (ER). To learn the segregation mechanisms of cathepsin E into its appropriate cellular destinations, the present studies were initiated to define the biosynthesis, processing, and intracellular localization as well as the site of proteolytic maturation of the enzyme in primary cultures of rat brain microglia. Immunohistochemical and immunoblot analyses revealed that cathepsin E was the most abundant in microglia among various brain cell types, where the enzyme existed predominantly as the mature enzyme. Immunoelectron microscopy studies showed the presence of the enzyme predominantly in the endosome-like vacuoles and partly in the vesicles located in the trans-Golgi area and the lumen of ER. In the primary cultured microglial cells labeled with [35S]methionine, 〉95% of labeled cathepsin E were represented by a 46-kDa polypeptide (reduced form) after a 30-min pulse. Most of it was proteolytically processed via a 44-kDa intermediate to a 42-kDa mature form within 4 h of chase. This processing was completely inhibited by bafilomycin A1, a specific inhibitor of vacuolar-type H+-ATPase. Brefeldin A, a blocker for the traffic of secretory proteins from the ER to the Golgi complex, also inhibited the processing of procathepsin E and enhanced its degradation. Procathepsin E, after pulse-labeling, showed complete susceptibility to endoglycosidase H, whereas the mature enzyme almost acquired resistance to endoglycosidases H as well as F. The present studies provide the first evidence that cathepsin E in microglia is first synthesized as the inactive precursor bearing high-mannose oligosaccharides and processed to the active mature enzyme with complex-type oligosaccharides via the intermediate form and that the final proteolytic maturation step occurs in endosome-like acidic compartments.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1471-4159.1998.70052045.x
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    Granulocyte medullasin levels in gingival crevicular fluid from chronic adult periodontitis patients and experimental gingivitis subjects (1990)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of periodontal research 25 (1990), S. 0 
    Details
    ISSN: 1600-0765
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: The concentration of medullasin, an elastase-like serine proteinase, in gingival crevicular fluid (GCF) from chronic adult periodontitis patients and experimental gingivitis subjects was determined by the highly sensitive immunoassay method. In periodontitis patients, the medullasin content increased with increase of the GCF volume and then attained a maximum value at a relatively mildly inflamed stage. The value was maintained through more serious stages of disease activity. However, the medullasin content was independent of the probing depth. The medullasin content of the patients was markedly decreased after periodontal treatment, indicating that the enzyme participates in the development of the chronic periodontitis. Large amounts of medullasin were also detected in GCF from experimental gingivitis subjects, although it was not detected by the activity measurements. There was a rapid increase in the medullasin content during the 4-day period after abstention from oral hygiene measures, which corresponded to those of severely inflamed periodontitis patients. The peak value decreased up to the 7th-d followed by a gradual increase during the 21-d experimental period. The increased medullasin level rapidly decreased following resumption of oral hygiene measures. The results suggest that medullasin plays important roles both in the defence mechanism against the gingival inflammation and in the development of the acute inflammation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1600-0765.1990.tb00927.x
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 4
    Electronic Resource
    Electronic Resource
    Cystatin activity in gingival crevicular fluid from periodontal disease patients measured by a new quantitative analysis method (1992)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of periodontal research 27 (1992), S. 0 
    Details
    ISSN: 1600-0765
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Cystatins are protein inhibitors of cysteine proteinases, which are believed to play an important role in the pathogenesis of periodontal disease. In this study, we report a new sensitive method for the quantitative analysis of cystatin activity in a small amount of crude sample such as gingival crevicular fluid. Cystatin activity in the crude sample was determined by using active site-titrated papain, which is a cysteine proteinase from the plant Carica papaya. Crude samples usually contain endogenous cysteine proteinases. These competed with the added papain for the active sites of the cystatins. The cystatin-cysteine proteinase complex was able to be dissociated by the addition of papain. This competition and dissociation could interfere with the determination of cystatin activity, since some of the cysteine proteinases, such as cathepsin B, hydrolyzed the specific substrate for papain during titration with the papain. In order to exclude this interference and measure total cystatin activity, the crude sample must be alkalinized (pH 11.0) for 5 min at 4°C followed by 10 min at 40°C before titration with papain. The minimum detectable amount of cystatins was 20 fmol/ assay when it was calculated per mole of papain inhibitory sites. Using this method, significant levels of cystatin activity were detected in all the samples of gingival crevicular fluid taken from periodontal disease patients. These results suggest that cystatins could regulate the cysteine proteinases in gingival crevicular fluid and that this new method could be useful to clarify the role of cystatins in the pathogenesis of periodontal disease.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1600-0765.1992.tb01813.x
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 5
    Electronic Resource
    Electronic Resource
    Cathepsins B, H and L activities in gingival crevicular fluid from chronic adult periodontitis patients and experimental gingivitis subjects (1990)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of periodontal research 25 (1990), S. 0 
    Details
    ISSN: 1600-0765
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: To clarify roles of lysosomal cysteine proteinases cathepsins B, H and L in pathological destructive process of periodontal tissues, levels of their enzymatic activities were determined in gingival crevicular fluid (GCF) from chronic adult periodontitis patients and from experimental gingivitis subjects. In periodontitis patients, higher levels of cathepsins B, H and L activities were found at sites with more serious signs of the disease activity. The total activity of each enzyme (per unit time) was positively correlated with the GCF volume. However, it had little or no correlation with the probing depth (PD). In contrast, the specific activity of each enzyme in GCF (activity units per mg protein), which reflects the selectivity of enzyme exudation, was negatively correlated with the GCF volume. These results suggest that the cysteine proteinases are selectively released into gingival crevices at a relatively mild stage of periodontitis. In experimental gingivitis subjects, no significant activity of each enzyme was detected in GCF, even when the quantity of GCF was comparable to that from periodontitis patients. These data suggest that no significant amounts of these enzymes are released at experimental gingivitis sites or that a homeostatic mechanism, including regulation by protease inhibitors, may control activities of these enzymes in GCF with acute inflammation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1600-0765.1990.tb00894.x
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 6
    Electronic Resource
    Electronic Resource
    Mineral phase in experimental ectopic calcification induced by lead acetate in the rat (1978)
    Springer
    Calcified tissue international 25 (1978), S. 69-74 
    Details
    ISSN: 1432-0827
    Keywords: Lead salt ; Ectopic calcification ; Lead pyrophosphate ; Apatite ; Transformation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Summary Experimental ectopic calcification caused by intravenous injection of lead acetate (Pb−Ac) followed by subcutaneous injection of polymyxin B sulfate (PMX) in the rat was studied by the methods of quantitative chemical analysis and X-ray diffraction analysis using samples freed of organic matter by low temperature ashing (LTA). In all specimens, X-ray diffraction data showed the presence of an apatitic phase. In addition, several unknown peaks, the intensities of which weakened with time, were found. These peaks were established to be those of lead pyrophosphate (Pb2P2O7) when compared with the Joint Committee on Powder Diffraction Standards (JCPDS), formerly the ASTM index. Improvements in crystallinity of the apatitic phase was accompanied by the increases in the amounts of calcium, phosphorus and carbonate in the LTA ash. The amount of magnesium, on the contrary, decreased from 3 to days. The molar Ca/P ratio was near to 1.5 up to 10 days and then increased to 1.59 at 40 days. When the LTA ash was heated at 600° C, the major crystal phase wasβ-tricalcium phosphate and the minor phase was hydroxyapatite up to 10 days; after that the relationship between the two phases was reversed. It is suggested that the characteristics of calcium phosphate in the native state was transformed between 10 and 20 days after administration of Pb−Ac and PMX.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02010753
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 7
    Electronic Resource
    Electronic Resource
    Synthesis of (Ba,Ca)(Zr,Ti)O〈sub〉3〈/sub〉 Ceramics from Ultra-Fine Precursors (2006)
    s.l. ; Stafa-Zurich, Switzerland
    Key engineering materials Vol. 301 (Jan. 2006), p. 235-238 
    Details
    ISSN: 1013-9826
    Source: Scientific.Net: Materials Science & Technology / Trans Tech Publications Archiv 1984-2008
    Topics: Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics
    Notes: Fine powder of CaZrO3 (CZ) was synthesized by using ultra-fine and highly dispersed CaCO3 as a precursor. The results showed that the calcination temperature could be reduced to inhibit grain growth of CZ. Mean grain size of the CZ fine powder was 80 nm. Moreover, the CZ powder was used to synthesize a solid solution of (Ba,Ca)(Zr,Ti)O3 (BCZT) to examine the effect of the powder’s grain size on the reactivity of BT and CZ. It was found that the fine CZ powder enhanced the BT and CZ reaction
    Type of Medium: Electronic Resource
    URL: http://www.tib-hannover.de/fulltexts/2011/0528/01/50/transtech_doi~10.4028%252Fwww.scientific.net%252FKEM.301.235.pdf
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 8
    Electronic Resource
    Electronic Resource
    Mechanism of induction of hypercalcemia and hyperphosphatemia by lead acetate in the rat (1977)
    Springer
    Calcified tissue international 24 (1977), S. 41-46 
    Details
    ISSN: 1432-0827
    Keywords: Lead salt ; Bone ; Mobilization ; Hypercalcemia ; Hyperphosphatemia
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Summary The present study is an investigation of the mechanism of hypercalcemia and hyperphosphatemia induced by the intravenous injection of lead acetate (Pb-Ac). A total of 118 male rats were injected with 30 mg/kg of Pb-Ac, or with 16.5 mg/kg of sodium acetate as the control. The levels of serum calcium, phosphorus and lead were then determined at various time periods after the injections. Serum calcium and phosphorus levels increased with time after Pb-Ac injection and the maximum values of calcium (17 mg%) were found after 1 h and of phosphorus (13.5 mg%) after 30 min. Both calcium and phosphorus levels reverted to the normal range after 12 h. The maximum net rates of increase of calcium and phosphorus were found immediately after Pb-Ac injection. At that time, deposition of lead at the calcifying sites of bone and incisor dentin was demonstrated by a histochemical examination. In other experiments the changes in the calcium and phosphorus contents in the medium after shaking bone powder in serum with Pb-Ac in an in vitro system were studied. It was confirmed that the calcium and phosphorus were displaced from the bone mineral, the extent of the displacement being correlated with the concentration of the Pb-Ac added to the medium, and that these displacements were very rapid reactions. These results suggest that hypercalcemia and hyperphosphatemia following Pb-Ac injection results from a direct action of lead on the bone mineral.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02223295
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 9
    Electronic Resource
    Electronic Resource
    Processing of NH2- and COOH-terminal peptides of rat osteocalcin by cathepsin B and cathepsin L (1998)
    Springer
    Journal of bone and mineral metabolism 16 (1998), S. 72-80 
    Details
    ISSN: 1435-5604
    Keywords: Key words: osteocalcin ; cathepsin B ; cathepsin L ; papain ; calcium-binding capability
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract: Rat osteocalcin was subjected to proteolysis by cathepsins B and L at acid pH in vitro. Short fragments of fewer than 8 amino acids were liberated from both the NH2- and COOH-termini of the molecule, but the midportion, composed of antiparallel α-helical domains, was resistant to proteolysis. Intact rat osteocalcin bound 10 Ca2+/mol protein at pH 7.5 and the binding decreased to half that amount at pH 5.0, while the midportion fragment (Ala8-Lys43) bound 4–5 Ca2+/mol protein at both pH 5.0 and 7.5. When COOH-terminal-truncated rat osteocalcin (Tyr1-Lys43) was prepared with lysyl-endopeptidase, it showed nearly the same Ca2+ binding as that of the intact molecule. Our results suggest that proteolytic processing of the terminal sequence of osteocalcin alters its intrinsic Ca2+-binding capacity and that its NH2-terminal sequence is probably involved.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s007740050029
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...