title: Acid phosphatase complex from the freshwater snail Viviparus viviparus L. under standard conditions and intoxication by cadmium ions.
abstract: Acid phosphatases differing in both subcellular localization and substrate specificity were isolated for the first time from the liver of the freshwater snail Viviparus viviparus L. by preparative isoelectrofocusing. One of five characterized phosphatases is highly specific to ADP and the others can hydrolyze (at variable rate) a series of natural substrates. A scheme is proposed for the involvement of the studied phosphatases in carbohydrate metabolism. We have also studied some peculiarities of the effect of Cd2+ in vitro and in vivo on the activities of individual components of the acid phosphatase complex and corresponding changes in metabolism of the freshwater snail as a new test-object allowing the estimation of toxicity in water.
authors.affiliation: Moscow Pedagogical State University, Moscow 119435, Russia. i_tsvetkoff@rambler.ru
authors.forename: I L
authors.initials: IL
authors.lastname: Tsvetkov
authors.forename: A P
authors.initials: AP
authors.lastname: Popov
authors.forename: A S
authors.initials: AS
authors.lastname: Konichev
mesh_terms: D000135:Acid Phosphatase / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism*; D000244:Adenosine Diphosphate / Q000378:metabolism; D000818:Animals; D002104:Cadmium / Q000633:toxicity*; D002412:Cations / Q000494:pharmacology; D006868:Hydrolysis; D008099:Liver / Q000166:cytology / Q000187:drug effects / Q000201:enzymology; D012908:Snails / Q000166:cytology / Q000187:drug effects* / Q000201:enzymology*; D013347:Subcellular Fractions / Q000201:enzymology; D013379:Substrate Specificity
chemical_list: D002412:Cations; D002104:Cadmium; D000244:Adenosine Diphosphate; D000135:Acid Phosphatase