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  • Key words Colorectal neoplasms  (1)
  • nicotinamide adenine dinucleotide, reduced form  (1)
  • Springer  (2)
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  • Springer  (2)
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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Journal of cancer research and clinical oncology 125 (1999), S. 357-360 
    ISSN: 1432-1335
    Keywords: Key words Colorectal neoplasms ; Apoptosis ; Chemosensitivity ; p53 gene
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Purpose : The p53 gene is considered one of the most important in the control of apoptosis, and its mutations have a close relationship with chemosensitivity. The aim of this work was to investigate the role of p53 in the apoptosis of colorectal cancer cells in vitro, induced by 5-fluorouracil (5-FU) and hydroxy-camptothecin (HCPT). Methods : A total of 39 colorectal cancer samples from patients were treated in vitro with 5-FU (10 μg/ml), 5-FU (10 μg/ml) + leucovorin (5 μg/ml), HCPT (0.1 μg/ml) and HCPT (0.1 μg/ml) + Salvia mitorrhiza (6 μl), using an in situ terminal deoxynucleotidyltransferase assay to detect chemosensitivity. p53 gene mutations from tumor DNA were detected, after amplification by the polymerase chain reaction of exons 5–8, by non-radioactive single-strand conformation polymorphism. Results : p53 gene mutations were observed in 43.6% (17/39) of colorectal carcinomas, when the terminal deoxynucleotidyltransferase assay was used to detect the tumor apoptotic rate. Cells with mutated p53 had lower chemosensitivity than those without (p 〈 0.01). Conclusion : Routine assessment of p53 status may be helpful in selecting patients with the wild-type p53 gene, who have a predictably better response to chemotherapy.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    The protein journal 16 (1997), S. 801-807 
    ISSN: 1573-4943
    Keywords: Lactate dehydrogenase ; NADH ; nicotinamide adenine dinucleotide, reduced form
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The kinetics of thermal inactivation of rabbit muscle lactate dehydrogenase at different temperatures has been studied using the kinetic method for the substrate reaction during irreversible inhibition of enzyme activity previously described by Tsou [Adv. Enzymol. Relat. Areas Mol. Biol. (1988), 61, 381–436]. The results show that thermal inactivation of the enzyme is an irreversible reaction. Microscopic rate constants were determined for thermal inactivation of the free enzyme and the enzyme–substrate complex. The inactivation rate constant of the free enzyme is much larger than the rate constant of the enzyme–substrate complex. The results suggest that the presence of the substrate has a certain protective effect against thermal inactivation of the enzyme.
    Type of Medium: Electronic Resource
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