Unknown

Dataset Information

0

A comparison of the properties of the pyruvate kinases of the fat body and flight muscle of the adult male desert locust.


ABSTRACT: 1. The pyruvate kinases of the desert locust fat body and flight muscle were partially purified by ammonium sulphate fractionation. 2. The fat-body enzyme is allosterically activated by very low (1mum) concentrations of fructose 1,6-diphosphate, whereas the flight-muscle enzyme is unaffected by this metabolite at physiological pH. 3. Flight-muscle pyruvate kinase is activated by preincubation at 25 degrees for 5min., whereas the fat-body enzyme is unaffected by such treatment. 4. Both enzymes require 1-2mm-ADP for maximal activity and are inhibited at higher concentrations. With the fat-body enzyme inhibition by ADP is prevented by the presence of fructose 1,6-diphosphate. 5. Both enzymes are inhibited by ATP, half-maximal inhibition occurring at about 5mm-ATP. With the fat-body enzyme ATP inhibition can be reversed by fructose 1,6-diphosphate. 6. The fat-body enzyme exhibits maximal activity at about pH7.2 and the activity decreases rapidly above this pH. This inactivation at high pH is not observed in the presence of fructose 1,6-diphosphate, i.e. maximum stimulating effects of fructose 1,6-diphosphate are observed at high pH. The flight-muscle enzyme exhibits two optima, one at about pH7.2 as with the fat-body enzyme and the other at about pH8.5. Stimulation of the enzyme activity by fructose 1,6-diphosphate was observed at pH8.5 and above.

SUBMITTER: Bailey E 

PROVIDER: S-EPMC1187519 | biostudies-other | 1969 Feb

REPOSITORIES: biostudies-other

Similar Datasets

| S-EPMC1187520 | biostudies-other
| S-EPMC1165786 | biostudies-other
2012-12-12 | GSE33898 | GEO
| S-EPMC4553487 | biostudies-literature
2012-12-12 | E-GEOD-33898 | biostudies-arrayexpress
| S-EPMC11310224 | biostudies-literature
2013-05-03 | GSE41214 | GEO
| S-EPMC4024192 | biostudies-literature
| S-EPMC5834936 | biostudies-literature
| S-EPMC5045875 | biostudies-literature