Enzymatic properties of fish muscle aldolase.
1. Aldolases were isolated from the ordinary muscle of red sea bream Pagrus major, Pacific mackerel Scomber japonicus, and carp Cyprinus carpio by ammonium sulfate fractionation, followed by ion-exchange chromatography on DEAE-cellulose and CM-Sepharose CL-6B columns, and examined for enzymatic properties. 2. The aldolases showed the highest activity in a pH range from 6.8-7.8 Km values for fructose-1,6-bisphosphate ranged from 0.025-0.10 mM. 3. Irrespective of fish species, aldolase activity was inhibited by ATP, ADP, and AMP. ATP showed the strongest inhibition and was competitive with fructose-1,6-bisphosphate. 4. The aldolases did not require divalent metal ions for activation and were completely inhibited at 0.1 mM Cu2+. 5. Thermal inactivation of the enzymes was of the first-order reaction. Red sea bream, Pacific mackerel and carp enzymes lost the activity by 50% when incubated at 50 degrees C for 8, 14 and 23 min, respectively.
Nakagawa
T
T
Department of Food Science and Technology, Faculty of Fisheries, Tokyo, University of Fisheries, Japan.
Nagayama
F
F
D000227:Adenine Nucleotides / Q000494:pharmacology; D000818:Animals; D002347:Carps / Q000378:metabolism; D002413:Cations, Divalent; D002852:Chromatography, Ion Exchange; D005399:Fishes / Q000378:metabolism*; D005634:Fructose-Bisphosphate Aldolase / Q000037:antagonists & inhibitors / Q000302:isolation & purification / Q000378:metabolism*; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D009132:Muscles / Q000201:enzymology*; D013045:Species Specificity
D000227:Adenine Nucleotides; D002413:Cations, Divalent; D005634:Fructose-Bisphosphate Aldolase