title: Carp liver DNase--isolation, further characterization and interaction with endogenous actin.
abstract: Deoxyribonuclease I (DNase I)-like enzyme from the liver of the carp (Cyprinus carpio) was purified to homogeneity and further characterized. Ion exchange chromatography on DEAE-cellulose, molecular filtration on Sephacryl S-300 and Con A-Sepharose affinity chromatography were applied for enzyme isolation. Carp liver DNase, similarly to DNase I from bovine pancreas, was found to be an endonuclease that hydrolyses linear DNA from salmon sperm as well as circular DNA forms--plasmid and cosmid. The purified enzyme is a glycoprotein and shows microheterogeneity, as observed in DNase zymograms prepared after native and two-dimensional electrophoresis (2D-PAGE). The composition of sugar component of the enzyme was characterized. Special attention was focused on the ability of carp liver DNase to interact with carp liver actin. The carp liver enzyme was inhibited by endogenous actin. The estimated binding constant of carp liver DNase to carp liver actin was calculated to be 1.1 x 10(6) M(-1).
authors.affiliation: Institute of Immunology and Experimental Therapy, Polish Academy of Sciences, R.Weigla 12, 53-114 Wroclaw, Poland.
authors.forename: Agnieszka
authors.initials: A
authors.lastname: Krawczenko
authors.forename: Lidia
authors.initials: L
authors.lastname: Ciszak
authors.forename: Maria
authors.initials: M
authors.lastname: Malicka-Blaszkiewicz
mesh_terms: D000199:Actins / Q000378:metabolism*; D000818:Animals; D002241:Carbohydrates / Q000737:chemistry; D002347:Carps; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D004247:DNA / Q000378:metabolism*; D003851:Deoxyribonucleases / Q000302:isolation & purification / Q000378:metabolism*; D015180:Electrophoresis, Gel, Two-Dimensional; D006023:Glycoproteins / Q000378:metabolism; D008099:Liver / Q000201:enzymology*
chemical_list: D000199:Actins; D002241:Carbohydrates; D006023:Glycoproteins; D004247:DNA; D003851:Deoxyribonucleases