[Purification and properties of ribonuclease from the eggs and embryos of the loach Misgurnus fossilis].
Endo- and exoribonucleases from loach eggs and embryos were partially purified. Endoribonuclease from loach embryos has a pH optimum of 8.4, is thermostable, has a molecular weight of about 37 000, requires Ca2+ for its activity, rapidly splits poly-U and slowly splits poly-C and does not hydrolyze poly-A. Exoribonuclease has a pH optimum of 7.6 and is relatively thermostable; its activity is independent of Ca2+, it has a molecular weight of 12 000, preferentially hydrolyzes RNA of yeast and poly-U, rather slowly hydrolyzes poly-C and does not split poly-A. The properties of the tested enzymes from loach embryos at early organogenesis do not differ from those of the enzymes from unfertilized eggs.
D000818:Animals; D004625:Embryo, Nonmammalian / Q000201:enzymology*; D005260:Female; D005399:Fishes; D007700:Kinetics; D008970:Molecular Weight; D010063:Ovum / Q000201:enzymology*; D012260:Ribonucleases / Q000302:isolation & purification* / Q000378:metabolism; D013379:Substrate Specificity
D012260:Ribonucleases
Vydelenie i nekotorye svoĭstva ribonukleaz iz iaĭtsekletok i zarodyshei v'iuna Misgurnus fossilis.