Isolation of human liver arginase cDNA and demonstration of nonhomology between the two human arginase genes |
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| Authors: | G J Dizikes W W Grody R M Kern S D Cederbaum |
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| Affiliation: | 1. Fujian Provincial Key Laboratory of Agroecological Processing and Safety Monitoring, College of Life Sciences, Fujian Agriculture and Forestry University, Fuzhou, Fujian 350002, China;2. Key Laboratory for Analytical Science of Food Safety and Biology of MOE, Fujian Provincial Key Lab of Analysis and Detection for Food Safety, College of Chemistry, Fuzhou University, Fuzhou, Fujian 350116, China;3. College of Resources and Environment, Fujian Agriculture and Forestry University, Fuzhou, Fujian 350002, China;1. Academic Unit of Anaesthesia, College of Medical, Veterinary and Life of Sciences–University of Glasgow, Royal Infirmary, Glasgow G31 2ER, UK;2. Academic Unit of Surgery, College of Medical, Veterinary and Life of Sciences–University of Glasgow, Royal Infirmary, Glasgow G31 2ER, UK;3. The Scottish Trace Element and Micronutrient Reference Laboratory, Department of Biochemistry, Royal Infirmary, Glasgow G31 2ER, UK;1. Wellcome Trust–MRC Cambridge Stem Cell Institute, Cambridge, United Kingdom;2. Department of Haematology, University of Cambridge, Cambridge, United Kingdom;3. Cambridge Institute for Medical Research, Cambridge Biomedical Campus, Cambridge, United Kingdom;4. Haematological Cancer Genetics, Wellcome Trust Sanger Institute–Hinxton, Cambridge, United Kingdom;5. MRC Cancer Unit, University of Cambridge, Hutchison/MRC Research Centre, Cambridge Biomedical Campus, Cambridge, United Kingdom;6. MRC Mitochondrial Biology Unit, University of Cambridge, Cambridge, United Kingdom |
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| Abstract: | A human liver cDNA library was screened by colony hybridization with a rat liver arginase cDNA. The number of positive clones detected was in agreement with the estimated abundance of arginase message in liver, and the identities of several of these clones were verified by hybrid-select translation, immunoprecipitation, and competition by purified arginase. The largest of these human liver arginase cDNAs was then used to detect arginase message on northern blots at levels consistent with the activities of liver arginase in the tissues and cells studied. The absence of a hybridization signal with mRNA from a cell line expressing only human kidney arginase demonstrated the lack of homology between the two human arginase genes and indicated considerable evolutionary divergence between these two loci. |
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