PubMed · 8030515
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M Sibley. 1994. Artificial tear issues.. https://doi.org/10.1007/978-1-4615-2417-5_76
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A method was developed for evaluating the specificity of the ion exchange chromatographic HbA1c method by Pharmacia which uses a Mono S column. To investigate hemoglobin fractions potentially interfering in HbA1c analysis, the chromatographic resolution was enhanced and a peak integration program was used which enables the quantitation of overlapping and even shoulder-like peaks. Hemoglobin was incubated with glucose in vitro and the chromatograms were analyzed before and after incubation. Five minor peaks were detected, close to hemoglobin A1c, which could not be conclusively identified as hemoglobins previously described. Four of these peaks, the stable ones, were included in the fraction of the chromatogram to be measured as HbA1c by the routine method. In practice, these peaks comprise 20%-35% of the routine HbA1c result in diabetic patients and 30%-45% in non-diabetic subjects. Three of these minor peaks were non-dependent on glucose. The chromatography and the peak integration method described can also be used to study hemoglobin adducts other than glycohemoglobin.
The bakers' yeast Saccharomyces cerevisiae contains a metallothionein (MT) gene family comprised of the amplified CUP1 locus and the single copy CRS5 gene. We demonstrate that CUP1 plays the dominant role in copper detoxification. A single copy of CUP1 was far more effective in conferring copper resistance than was CRS5. The CUP1 promoter contributes to this resistance; in a promoter exchange experiment, the Crs5 MT conferred strong copper resistance when its expression was driven by the CUP1 promoter, and conversely, the CRS5 promoter reduced the effectiveness of Cup1 MT. Unlike CUP1, the CRS5 promoter appears to be refractory to high concentrations of copper. The CUP1 coding sequences also contribute to copper tolerance, presumably reflecting the enhanced binding avidity of Cup1 MT for Cu(I) ions. In studies with the bathocuproine Cu(I) chelator, the Cu(I) ions bound to Crs5 were kinetically more labile than the Cu(I) binding to Cup1. Our findings are consistent with the assembly of Crs5 into two metal-binding clusters, similar to mammalian MTs, but unlike Cup1. Overall, the striking differences in gene structure, regulation, and function of CUP1 and CRS5 are remarkably reminiscent of the MTI and MTII genes of the pathogenic yeast Candida glabrata.
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