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James W. Hogan

Publications and source records attributed to James W. Hogan.

7 recordsLinked to original sources
USGS1969

Laboratory studies on antimycin A as a fish toxicant

Liquid and sand formulations of antimycin A were tested in laboratory waters of various temperature, hardness, pH, and turbidity against 31 species of fresh-water fish of various sizes and life stages. Each formulation of toxicant was lethal under all water conditions to fish eggs, fry, fingerlings, and adult fish. Trouts are the most sensitive and catfishes the least sensitive. Of the 31 species, 24 succumb to 5 p.p.b. or less of the toxicant; only certain catfishes survive 25 p.p.b, The order of toxicity to various species of fish suggests that antimycin has possibilities for selective or partial control of certain unwanted fish. Although toxic to fish under ice, antimycin is more active in warm water than in cold. It is slightly more active in soft water than in hard; it is more active and persists far longer in water at pH 5 to 8 than at pH 9 or 10. It is active on fish in either clear and turbid waters, and it can be detoxified by potassium permanganate, The results contributed to registration of antimycin A in Fintrol-5 formulation as a fish toxicant.

Investigations in Fish Control↗
USGS1968

Some enzymatic properties of brain Acetylcholinesterase from bluegill and channel catfish

Using a manometric technique an acetylcholinesterase (EC 3.1.1.7, acetylcholine acetyl-hydrolase) was demonstrated in brain tissue from the bluegill, Lepomis macrochirus Rafinesque, and the channel catfish, Ictalurus punctatus (Walbaum). The activities were 19 and 37 μmoles acetylcholine hydrolyzed/milligram protein per hour for the bluegill and channel catfish enzymes, respectively. The optimum substrate concentration for the hydrolysis of acetylcholine was 10 m M for the enzymes from both species. Generally, the catfish acetylcholinesterase was somewhat more susceptible than the bluegill to the inhibitors tested; however, the bluegill enzyme was more susceptible to inhibition by malathion and malaoxon.

Journal of the Fisheries Research Board of Canada↗
USGS1968

Electrophoretic separation of fish brain esterases

Fish brains were homogenized in an all-glass Potter-Elvehjem-type tissue grinder in 40% sucrose solution. The homogenate concentration was 10 brains/ml for both the bluegill and channel catfish. The brei was centrifuged at 34,700 g for 30 min at 5 C, and 30 J.lliters of the supernatant were used per column for electrophoresis.

Journal of the Fisheries Research Board of Canada↗
USGS1968

Degradation of organophosphates by fish liver phosphatases

Liver homogenates of bluegill, Lepomis macrochirus Rafinesque, and channel catfish, Ictalurus punctatus (Walbaum), were shown by a manometric technique to contain soluble enzymes capable of degrading di iso propyl phosphorofluoridate (DFP) and 2,2-dichlorovinyl dimethyl phosphate (dichlorvos). Hydrolysis of the compounds was greatest in the presence of the manganic ion. Tentative identification of certain of the hydrolysis products suggested that cleavage of the anhydride bond was a degradation pathway for DFP and dichlorvos in vitro under the assay conditions employed. Substrate summation, inhibition, and activation experiments failed to clearly indicate more than a single enzyme hydrolyzing DFP and dichlorvos in the two fish.

Journal of the Fisheries Research Board of Canada↗