Determination of isocitrate lyase and malate synthase activities in a marine bivalve mollusk by a new method of assay.
1. A new method for the assay of isocitrate lyase (EC 4.1.3.1) was developed, based on the isolation of 14C-glyoxylate semicarbazone by co-crystallization with authentic carrier. The method was easily adapted to measure malate synthase (EC 4.1.3.2). 2. Interfering reactions were avoided with this method, and isocitrate dehydrogenase (ID) was easily distinguished from isocitrate lyase (IL). Assay of IL in germinating pumpkin seeds gave rates proportional to the amount of extract, with greater sensitivity and less variability than the spectrophotometric method. 3. Six species of marine bivalve mollusks were tested for IL activity, and two species produced glyoxylate: Crassostrea virginica at 0.10 mumol/hr/g tissue, and Petricola pholadiformis at 0.85 mumol/hr/g. The other four species, and four other marine invertebrates from other phyla, lacked detectable IL activity. 4. The rate of disappearance of glyoxylate in the malate synthase (MS) reaction indicated that Petricola had an activity of 0.60 mumol/hr/g: this is the first demonstration of activities of both IL and MS in a marine invertebrate.
Benevides
J M
JM
Department of Zoology, University of Rhode Island, Kingston 02881.
Tremblay
G C
GC
Hammen
C S
CS
D000818:Animals; D007522:Isocitrate Lyase / Q000032:analysis*; D008292:Malate Synthase / Q000032:analysis*; D008974:Mollusca / Q000201:enzymology*; D007652:Oxo-Acid-Lyases / Q000032:analysis*; D011874:Radiometry; D013056:Spectrophotometry, Ultraviolet
D008292:Malate Synthase; D007652:Oxo-Acid-Lyases; D007522:Isocitrate Lyase