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Biochemical characterization of phosphoglucose isomerase and genetic variants from mouse andDrosophila melanogaster

โœ Scribed by Daniel Charles; Chi-Yu Lee


Publisher
Springer
Year
1980
Tongue
English
Weight
722 KB
Volume
29
Category
Article
ISSN
0300-8177

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๐Ÿ“œ SIMILAR VOLUMES


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โœ Daniel J. Charles; Chi-Yu Lee ๐Ÿ“‚ Article ๐Ÿ“… 1980 ๐Ÿ› Springer ๐ŸŒ English โš– 835 KB

Two electrophoretic variants of phosphoglucose isomerase ( PGI) were purified from whole body extracts of DBA/2J and C5 7BL/6Jmice by a substrate-affinity elution from an 8-(6-aminohexyl) amino-A TP-Sepharose column followed by preparative isoelectric focusing. Both PGI variants were shown to be dim

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The allozymes involved in a one-locus, two-allele polymorphism for phosphoglucose isomerase from populations of the sea anemone Metridium senile from the northeast coast of North America exhibit different heat stabilities. The electrophoretically slow form is more stable than the fast, whether or no

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โœ Chi-Yu Lee; Bruna Pegoraro ๐Ÿ“‚ Article ๐Ÿ“… 1979 ๐Ÿ› Springer ๐ŸŒ English โš– 666 KB

Three electrophoretic variants of 3-phosphoglycerate kinase 2 (PGK-2A,PGK-2B, and PGK-2C) were purified from DBA/2J, C3H/HeJ, and C57L/J mice, respectively. PGK-2C exhibits only 2% of the specific activity of PGK-2A and PGK-2B in the reaction leading to the formation of 1,3-diphosphoglycerate. Compa