title: Enzymatic properties of fish muscle aldolase.
abstract: 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.
authors.affiliation: Department of Food Science and Technology, Faculty of Fisheries, Tokyo, University of Fisheries, Japan.
authors.forename: T
authors.initials: T
authors.lastname: Nakagawa
authors.forename: F
authors.initials: F
authors.lastname: Nagayama
mesh_terms: 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
chemical_list: D000227:Adenine Nucleotides; D002413:Cations, Divalent; D005634:Fructose-Bisphosphate Aldolase