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- W1520257872 abstract "Abstract 1. 1. Chicken muscle and chicken liver fructose-1,6-diphosphatases ( d -fructose-1,6-diphosphate 1-phosphohydrolase, EC 3.1.3.11) have been purified. The enzymes were found to be homogeneous according to several criteria including purification to a constant specific activity, electrophoresis on cellulose acetate strips, absence of other glycolytic enzyme activities, and sedimentation velocity studies. The chicken liver enzyme was also tested for homogeneity by immunodiffusion on agar and by crystallization. 2. 2. Comparisons of the two enzymes show that they have similar ultraviolet light absorption spectra but differ with respect to several other properties. The specific activity of the pure muscle enzyme is higher than that of the pure liver enzyme. Electrophoresis in several buffers and isoelectric point determinations (liver, 8.1 and muscle, 8.6) indicate that the avian enzymes differ in their electrostatic natures. The muscle enzyme (s20,w of 7.0) sediments at a slightly faster rate than the liver enzyme (s20,w of 6.8). Immunological analysis by double diffusion on agar and quantitative precipitin tests with anti-serum to chicken liver fructose-1,6-diphosphatase indicate that the liver and breast muscle enzymes differ immunologically. Kidney fructose-1,6-diphosphatase, in contrast, is immunologically similar to the liver enzyme. The anti-serum readily cross-reacts with other avian fructose-1,6-diphosphatases (turkey and budgerigar) but not with mammalian liver fructose-1,6-diphosphatases (rat and rabbit). The differences in properties of chicken liver and chicken breast muscle fructose-1,6-diphosphatases and immunological similarity of chicken liver and kidney fructose-1,6-diphosphatases suggest that there are at least two isozymic forms of avian fructose-1,6-diphosphatases." @default.
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- W1520257872 date "1972-05-01" @default.
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- W1520257872 title "Avian fructose-1,6-diphosphatases" @default.
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- W1520257872 doi "https://doi.org/10.1016/0005-2744(72)90341-5" @default.
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