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  • 11
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    Unknown
    Urbana, etc. : Periodicals Archive Online (PAO)
    American Journal of Psychology. 63:3 (1950:July) 453 
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  • 12
    facet.materialart.
    Unknown
    Urbana, etc. : Periodicals Archive Online (PAO)
    American Journal of Psychology. 66:1 (1953:Jan.) 144 
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  • 13
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Group
    Nature 289 (1981), S. 688-690 
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Washed, fixed and non-fixed platelets were examined for thrombin-enhanced agglutinin activity using microtitre plates (Table 1). It is known that non-activated platelets do not express the agglutinin5, and accordingly non-activated washed platelets did not agglutinate either themselves or fixed ...
    Type of Medium: Electronic Resource
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  • 14
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Group
    Nature 214 (1967), S. 1342-1343 
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Sylvn et al.4-6 have also provided evidence that proteolytic enzymes, especially the cathepsins, may be released from viable malignant tumour cells. This release may be an integral part of the metabolism of these cells: the extracellular cathepsin activity probably accounts for much of their ...
    Type of Medium: Electronic Resource
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  • 15
    ISSN: 1432-0843
    Keywords: Key words LY355703  ;  Cryptophycin  ;  Antimitotic  ; Oncolytic  ;  Cell cycle
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Purpose: Cryptophycin 52 (LY355703) is a new member of the cryptophycin family of antitumor agents that is currently undergoing clinical evaluation for cancer chemotherapy. The mechanism of action of the cryptophycin class of compounds is associated with an action on microtubules. This report details the pharmacological profile of this new clinical compound in a panel of human tumor cell lines. Methods: Antiproliferative effects of cryptophycin 52 were measured indirectly by detection of the metabolic reduction of alamarBlue®. Cytoxicity was assessed by enzymatic dye activation (calcein AM) combined with dye exclusion (ethidium homodimer) and by clonogenicity assay. Cell cycle effects were evaluated using flow cytometry and fluorescence microscopy. Results: Both antiproliferative and cytotoxic effects of cryptophycin 52 were concentration- and time-dependent. IC50 values for antiproliferative activity in both solid and hematologic tumor cell lines were in the low picomolar range, and without exception, were significantly below values for the antimitotic agents paclitaxel and vinblastine. Flow cytometry and microscopic examination of tumor cells treated with cryptophycin 52 indicated that they accumulated in the mitotic phase of the cell cycle. Cryptophycin 52 was tested for its sensitivity to multidrug-resistance in several paired cell lines in which a sensitive parental line was matched with a multidrug-resistant derivative line. The resistant lines have been shown to over express Pgp and/or MRP multidrug-resistance transport factors. Compared to other antimitotic agents (paclitaxel, vinblastine, vincristine), the potency of cryptophycin 52 was shown to be minimally affected in multidrug-resistant cells compared to their sensitive parental lines. Conclusion: Cryptophycin 52 has potent antimitotic, antiproliferative and cytotoxic activity in in vitro human tumor cell models. It is significantly more potent and less sensitive to multidrug resistance mechanisms than other antimitotic antitumor agents currently used in cancer therapy. These characteristics may translate into therapeutic advantages for the clinical use of cryptophycin 52 in cancer chemotherapy.
    Type of Medium: Electronic Resource
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  • 16
    ISSN: 1432-1793
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract In general, variance in tissue hydrolase (amylase, cellulase and protease) activity between individuals of a particular species is as great or greater than variance between tissue types or between species, e.g. although the specific activity of amylase in the gut tissue ofDendraster excentricus is significantly lower than that of aboral surface tissue, it is not significantly different than that of the oral surface tissue, or of the aboral surface of eitherPisaster ochraceus orStrongylocentrotus droebachiensis. Cellulase activity of the gut tissue ofS. droebachiensis was significantly higher than that of the gut tissue ofP. ochraceus andD. excentricus, reflecting the omnivorous feeding habit of the sea urchin. Cellulase activity of the gut tissue ofD. excentricus was not significantly higher than inP. ochraceus, an unexpected result, given the highly carnivorous behavior of the latter. Protease activity of the gut tissue ofD. excentricus is significantly higher than that of the oral or aboral surface tissues, but not significantly higher than that of the gut tissues ofP. ochraceus orS. droebachiensis. Amylase and cellulase activities in the guts of detritus- and shrimp-fedD. excentricus showed significant increases over that of field individuals; protease activity displayed no significant increase. Some significant surface (oral and aboral) changes were noted with respect to hydrolase activity, but the direction and lack of consistency of the changes argues that these are incidental to the process of digestion. The lack of significant differences in the surface enzyme activity ofD. excentricus, P. ochraceus andS. droebachiensis suggests that macronutrient digestive events in surface tissues are not uniquely important inD. excentricus.
    Type of Medium: Electronic Resource
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  • 17
    Electronic Resource
    Electronic Resource
    Springer
    Marine biology 123 (1995), S. 735-740 
    ISSN: 1432-1793
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Specimens of Pisaster ochraceus, an intertidal carnivorous seastar, were collected in northern Puget Sound at Post Point, near Bellingham, Washington, USA, in November 1993, and used in experimentation through September 1994. Ammonium sulfate fractions (60% precipitates) from excised pyloric caeca (digestive glands) possessed β-glucanase activity directed toward such β-linked substrates as carboxymethylcellulose (CMC), partially-digested cellulose (cellodextrins) and the synthetic substrate p-nitrophenyl-β-D-glucoside (PNDG). pH-activity and pH-stability maxima were at pH 6 and 5, respectively. No hydrolytic activity was detectable on native cellulose, native chitin or on cationic-modified celluloses such as DEAE-cellulose. Gel filtration (Sephadex G-100) of this 60% precipitate followed by DEAE-Sephadex column chromatography revealed heterogeneity of β-glucanase activity, with an indication of up to 11 distinct fractions with variable activity directed toward the substrates indicated above (CMC, cellodextrins and PNDG). These fractions displayed differing ratios of hydrolytic activity on these substrates. None of the isolated fractions displayed activity toward either native cellulose or native chitin. Gut extracts from the edible mussel (Mytilus edulis), a common prey species of P. ochraceus, were shown to possess partially digested cellulose (cellodextrins). These cellodextrins were further degraded by seastar β-glucanases in vitro. The digestion of the gut contents of ingested prey provides a possible adaptive explanation for the presence of β-glucanase activity in a carnivore.
    Type of Medium: Electronic Resource
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  • 18
    ISSN: 1432-1793
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Pisaster ochraceus were collected at Post Point, Bellingham, Washington, USA, in 1980. Total protease and tryptic specific activities were measured in pyloric caecal tissues and pyloric duct fluids of fed and starved individuals. Feeding resulted in increased levels of total protease and tryptic activities, and led to an increase in the ratio of total protease to tryptic specific activity in pyloric caecal tissue and a decrease in that ratio in pyloric duct fluid, indicating a release of trypsin into the duct with feeding. Trypsin activity showed little variability in fed seastars, but was quite variable in starving individuals. Total proteolytic acitivity, unlike that of tryptic activity, was always present in both fed and starved seastars. This way indicate a much broader role of generalized proteases in the cells of the pyloric caecum (e.g. as lysosomal enzymes of absorptive cells) in comparison to tryptic enzymes.
    Type of Medium: Electronic Resource
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  • 19
    Electronic Resource
    Electronic Resource
    Springer
    Marine biology 29 (1975), S. 261-266 
    ISSN: 1432-1793
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The purple seastar Pisaster ochraceus contains clearly measurable protease and amylase activity. Centrifuged supernatants of pyloric caeca homogenates undergo a spontaneous threefold increase in protease activity when incubated under toluene for 50 h at 25°C. Amylase activity remains nearly constant over this period. Bovine trypsin at a 1 to 100 ratio (trypsin to supernatant protein) induces a twofold increase in protease activity over that of the control supernatant while having virtually no effect on amylase activity over the control. The data indicate a specific interaction of trypsin with a protease zymogen rather than a conspecific hydrolysis of membrane components or vesicles by trypsin. Two percent Triton X-100 used as a diluent in place of distilled, deionized water causes a sevenfold increase in protease activity and a twofold increase in amylase activity in pyloric caeca supernatants. The use of Triton as a diluent in the preparation of a stomach-tissue supernatant allows quantitative measurement of both protease and amylase activity in that tissue.
    Type of Medium: Electronic Resource
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  • 20
    ISSN: 1432-1793
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract An investigation of enzymatic activity in the pyloric caeca of Pisaster ochraceus collected at Post Point, Bellingham, Washington, USA, in 1982, revealed the presence of four distinct proteases. These enzymes have been partially purified and characterized and display tryptic, chymotryptic and carboxypeptidase A-like activity. The two distinctive tryptic enzymes have molecular weights of 88 000 and 25 200 daltons, respectively, as determined by reducting SDS-PAGE electrophoresis. The chymotryptic and carboxypeptidase A proteases have molecular weights of 22 800 and 34 400 daltons, respectively. The tryptic and chymotryptic enzymes are inactivated by phenylmethylsulfonyl fluoride, indicating that all are serine proteases. Both trypsins are inhibited by soybean trypsin inhibitor; however, the high molecular weight trypsin was not inhibited by tosyl-L-lysine chloromethyl ketone. The chymotrypsin was inhibited by tosyl-L-phenylalanine chloromethyl ketone. Both reagents indicate the involvement of histidine in the active site. The low molecular weight trypsin and the chymotrypsin were able to activate bovine trypsinogen to trypsin, as determined in a modified PAGE electrophoresis with trypsinogen and casein copolymerized in the gel.
    Type of Medium: Electronic Resource
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