Survey of isoenzymes in the snail Cepaea nemoralis using different buffer/gel systems in polyacrylamide disc gel electrophoresis: validity of comparisons and effect of "nothing dehydrogenase" activity.
An investigation into isoenzymic analysis using four different buffer/gel systems was carried out. Fourteen different isoenzyme systems were surveyed on each buffer/gel system. It is shown that comparable results are not obtained between different systems. Previous workers in Cepaea nemoralis have used different buffer/gel systems from one another. Alkaline phosphatase and acid phosphatase and certain lactate and malate dehydrogenases are shown to behave similarly in three different systems. It is tentatively suggested that these isoenzymes may be genetically identical. "Nothing dehydrogenase" activity is demonstrated in gels stained for other dehydrogenases. It is suggested that nothing dehydrogenase activity may be attributable to glutamate or malate dehydrogenase.
D000135:Acid Phosphatase / Q000235:genetics*; D000469:Alkaline Phosphatase / Q000235:genetics*; D000818:Animals; D002021:Buffers; D004591:Electrophoresis, Polyacrylamide Gel; D007770:L-Lactate Dehydrogenase / Q000235:genetics*; D008291:Malate Dehydrogenase / Q000235:genetics*; D011110:Polymorphism, Genetic; D012908:Snails / Q000235:genetics*; D013379:Substrate Specificity
D002021:Buffers; D007770:L-Lactate Dehydrogenase; D008291:Malate Dehydrogenase; D000469:Alkaline Phosphatase; D000135:Acid Phosphatase