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  • 1985-1989  (3)
  • Life and Medical Sciences  (2)
  • DNA  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Intracellular lactate dehydrogenase concentration as an index of cytotoxicity in rat hepatocyte primary culture (1988)
    Springer
    Cell biology and toxicology 4 (1988), S. 1-11 
    Details
    ISSN: 1573-6822
    Keywords: DNA ; hepatocyte ; IC50 ; LDH ; monolayer ; protein
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract In searching for a reliable index for cytotoxicity testing in rat hepatocyte primary culture, lactate dehydrogenase (LDH) concentrations in lysates of attached hepatocytes and LDH released into the culture medium were compared under conditions of exposure to various dosages of sodium chloride, sodium salicylate, R-warfarin, acetaminophen, phenylbutazone, and furosemide (frusemide). The amount of intracellular LDH was assessed by inducing the cells to release the enzyme with 0.1% Tritron X-100. The induced LDH leakage was completed in 1 hr and the LDH activity was stable in storage at 10° for 2 weeks. We found that intracellular LDH is a direct indicator of the number of viable hepatocytes in contrast to the LDH released, because released LDH does not account for the significant number of cells detached from monolayer but which are not leaky, during the 6-hr test period. Based on IC50 values (50% inhibitory concentration), the relative cytotoxicities are R-warfarin 〉 phenylbutazone 〉 furosemide 〉 acetaminophen 〉 sodium salicylate 〉 sodium chloride.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00141283
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Role of glandular kallikreins as growth factor processing enzymes: Structural and evolutionary considerations (1987)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 33 (1987), S. 65-75 
    Details
    ISSN: 0730-2312
    Keywords: precursor ; hormone ; limited proteolysis ; submandibular gland ; prostate ; nerve growth factor ; epidermal growth factor ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Hormones and growth factors are generally released from larger precursors by limited proteolysis. The causative agents remain poorly defined with respect to location and properties. One subset of proteases, the glandular kallikreins, have been implicated in a few cases, in part because of their specific association with mature forms of some hormones. However, limited distribution and low copy number in some species cast doubt on this hypothesis, and they may well play other physiological functions that remain to be elucidated.
    Additional Material: 2 Tab.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcb.240330107
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Nerve growth factor biosynthesis: Isolation and characterization of a guinea pig prostate kallikrein (1985)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 29 (1985), S. 309-319 
    Details
    ISSN: 0730-2312
    Keywords: guinea pig ; kallikrein ; nerve growth-factor ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Guinea pig prostate contains one major soluble esteropeptidase activity. The protein has been purified and characterized and found to be a glycoprotein comprised of a single polypeptide chain. The molecular weight of the deglycosylated protein is approximately 26,000. The esteropeptidase has a similar Km for lysine and arginine synthetic substrates, although the Vmax for arginine is much greater than that for lysine. Amino-terminal sequence analysis has also revealed a marked degree of homology to mouse γ-nerve growth factor (NGF) and the kallikrein family of serine proteases. In contrast to γ-NGF, however, the guinea pig enzyme does not appear to form stable complexes with β-NGF.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcb.240290405
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    Paper (German National Licenses)
    Fulltext
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