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Mol Biol (Mosk) ; 25(6): 1546-64, 1991.
Article in Russian | MEDLINE | ID: mdl-1726019

ABSTRACT

Amylose isomerase (AI) preparations were isolated from rabbit muscles after Petrova et al., as well as by the additional fractionation steps. Their homogeneity, enzymatic activity and RNA, isolated from those preparations, were characterized. AI preparations, as described by Petrova et al., proved to be heterogeneous in respect to the protein and RNA; by using additional fractionation methods RNA and protein have been separated from each other, which proves that a homogeneous stable ribonucleoprotein complex, exerting AI activity, does not exist. It was shown by three independent methods that AI preparations isolated after Petrova do not display branching, but have amylolytic activity. RNA, isolated along with the AI preparations, proved to be mainly total tRNA degraded to different degrees. No RNA corresponding to the previously sequenced 2.5S RNA could be detected in these preparations. RNA preparations do not manifest neither branching, nor amylolytic activity. Our data prove that there is no ribozyme, whose existence has been suggested previously.


Subject(s)
1,4-alpha-Glucan Branching Enzyme/metabolism , Muscles/enzymology , RNA, Catalytic/metabolism , Ribonucleoproteins/metabolism , 1,4-alpha-Glucan Branching Enzyme/genetics , Animals , Base Sequence , Chromatography, Gel , Electrophoresis, Polyacrylamide Gel , Molecular Sequence Data , RNA/genetics , Rabbits
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