Localization of two glycolytic enzymes in guinea-pig taenia coli.
The bound fractions of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and of fructose 1,6-diphosphate aldolase (ALD) were measured in intact Taenia coli. ALD was approximately 60% bound and GAPDH was approximately 41% bound. Bound ALD activity remaining in chemically demembranated Taenia coli was similar to that in intact tissue indicating a localization to the contractile apparatus. ALD was found to be specifically bound in the demembranated preparation. Chemical demembranation resulted in almost complete loss of all GAPDH activity indicating a localization of bound GAPDH to cellular membranes.
Hardin
C D
CD
Department of Physiology and Biophysics, University of Cincinnati, OH.
Paul
R J
RJ
D000818:Animals; D002462:Cell Membrane / Q000201:enzymology; D003106:Colon / Q000201:enzymology*; D005634:Fructose-Bisphosphate Aldolase / Q000378:metabolism*; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000378:metabolism*; D006168:Guinea Pigs
D005987:Glyceraldehyde-3-Phosphate Dehydrogenases; D005634:Fructose-Bisphosphate Aldolase