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  • Articles  (2)
  • Life and Medical Sciences  (1)
  • bottled water  (1)
  • 1
    ISSN: 1573-2932
    Keywords: bottled water ; bacteriological quality and physico-chemicalquality
    Source: Springer Online Journal Archives 1860-2000
    Topics: Energy, Environment Protection, Nuclear Power Engineering
    Notes: Abstract Bacteriological and physico-chemical parameters of 265 samples from 39 brands sold in 5-gallon plastic and glass bottles and 2-5 L plastic containers were analyzed to determine the quality of bottled water distributed in Mexico City. Tests included fecal and total coliform counts, alkalinity, total hardness, chloride, calcium and magnesium concentrations, pH and conductivity. Correlation and cluster analyses and ANOVA were carried out, and a comparison made of the averages with the maximum permissible levels established in the Official Mexican Norms. Concerning the investigated parameters no differences (p 〉 0.05) between the brands were found. Physico-chemical parameters were studied and all the samples were within the permissible limits. Most samples taken from the 5-gallon containers exceeded the maximum bacteriological limits. It was concluded that the bacteriological quality of the brands studied was extremely variable. Appropriate sanitary measures, should be established to control this aspect.
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  • 2
    ISSN: 0749-503X
    Keywords: chitin synthase III ; morphogenesis ; Calcofluor resistance ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: We have cloned CHS4, a gene that complements the resistance to Calcofluor of the Saccharomyces cerevisiae cal2 mutant. We show that CHS4 is allelic to the previously described SKT5 and CSD4 genes. CHS4 encodes a 696 amino acids protein with no potential transmembrane domain. chs4-null mutants are resistant to Calcofluor white and exhibit a considerable reduction in cell wall chitin and in chitin synthase III (CSIII) activity. Biochemical characterization of chitin synthase III from these null mutants indicates that the defect is due to a reduced Vmax of the enzyme. This defect can be overcome in vitro by trypsin treatment of the membrane preparations. Chs4p does not act as a transcriptional or translational regulator of CHS3, the gene coding for the catalytic subunit of CSIII activity, and we therefore propose that Chs4p would be an essential component of the CSIII complex, acting as a post-translational regulator of this activity. In addition to the chitin defect, the chs4 mutant shows a severe defect in mating. © 1997 John Wiley & Sons, Ltd.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
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