Effect of glutaraldehyde and lead on the activity of hepatic glucose-6-phosphatase. A biochemical and cytochemical study.
The sensitivity of mouse liver glucose-6-phosphatase activity towards glutaraldehyde fixation has been analysed by biochemical and cytochemical means. The degree of enzymatic inhibition and various enzymatic properties have been studied. Several differences have been observed in the Km determination, the sensitivity to pH 5 and the activity related to pH between fixed and unfixed enzymes. The role of Pb++ ions in the cytochemical media has also been estimated. It is concluded that several enzymatic differences appear between fixed and unfixed enzymes and that the inhibition by Pb ions is dependent on the buffer and on the amount of substrate used.
D000447:Aldehydes / Q000494:pharmacology*; D000818:Animals; D002021:Buffers; D004721:Endoplasmic Reticulum / Q000201:enzymology / Q000648:ultrastructure; D005952:Glucose-6-Phosphatase / Q000032:analysis* / Q000037:antagonists & inhibitors; D005976:Glutaral / Q000494:pharmacology*; D006651:Histocytochemistry / Q000379:methods; D006652:Histological Techniques; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D007854:Lead / Q000494:pharmacology*; D008099:Liver / Q000201:enzymology* / Q000648:ultrastructure; D008297:Male; D051379:Mice; D008813:Mice, Inbred ICR; D010477:Perfusion / Q000379:methods
D000447:Aldehydes; D002021:Buffers; D007854:Lead; D005952:Glucose-6-Phosphatase; D005976:Glutaral