Glutamine phosphoribosylpyrophosphate amidotransferase from Escherichia coli. Purification and properties.
LJ Messenger, H Zalkin - Journal of Biological Chemistry, 1979 - ASBMB
Glutamine 5-phosphoribosylamine: pyrophosphate phosphoribosyltransferase
(amidophosphoribosyl-transferase) has been purified to homogeneity from Escherichia coli.
The molecular weight of the native enzyme was 194,000 by sedimentation equilibrium
centrifugation and 224,000 by gel filtration. A subunit Mr= 57,000 was estimated by gel
electrophoresis in sodium dodecyl sulfate. Cross-linking experiments gave species of Mr=
57,000, 117,000, and 177,000. A trimer or tetramer of identical subunits is indicated for the …
(amidophosphoribosyl-transferase) has been purified to homogeneity from Escherichia coli.
The molecular weight of the native enzyme was 194,000 by sedimentation equilibrium
centrifugation and 224,000 by gel filtration. A subunit Mr= 57,000 was estimated by gel
electrophoresis in sodium dodecyl sulfate. Cross-linking experiments gave species of Mr=
57,000, 117,000, and 177,000. A trimer or tetramer of identical subunits is indicated for the …
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