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T A Shvedova

Publications and source records attributed to T A Shvedova.

12 recordsLinked to original sources
PubMed1987

Catalytic activity of the nucleic acid component of the 1,4-alpha-glucan branching enzyme from rabbit muscles.

2.5 S RNA, the nucleic acid component of the 1,4-alpha-D-glucan: 1,4-alpha-D-glucan 6-alpha-(1,4-alpha-glucano)-transferase from rabbit muscles, devoid of any protein, catalyses the branching reaction, as does the holoenzyme. The conclusion is drawn that 2.5 S RNA is a ribozyme. To get an insight into the significance of different parts of the molecule for the catalytic activity of 2.5 S RNA, a large fragment isolated from its partial RNAase A digest was investigated. This fragment which proved to be the middle part of polyribonucleotide chain containing all modified nucleotides exerts some catalytic activity, too.

1,4-alpha-Glucan Branching Enzyme↗
PubMedDate not supplied

[Isolation and properties of preparations the branching enzyme of muscles, amylose isomerase].

The paper describes a modified method of isolating the branching enzyme of amylose isomerase from muscles and a study of the enzyme activity at different stages of purification. By enzyme fractionation on biogel R-150 and Sepharose 6B the fractions containing different RNA amounts have been isolated. The activity of fractions has been shown to depend on their content of RNA. The paper presents a procedure used to isolate a highly purified fraction of amylose isomerase and its properties (pH and temperature optima, enzyme optimal concentration and Michaelis constant).

1,4-alpha-Glucan Branching Enzyme↗
PubMedDate not supplied

[Structure-function study of 1,4-alpha-glucan branching enzyme by limited trypsin treatment].

1.4-alpha-glucan branching enzyme (EC 2.4.1.18) from rabbit muscles with an essential 2.5S RNA component has been studied by limited trypsin treatment. Under a great variety of hydrolysis conditions the product resistant to subsequent action of trypsin was obtained. This product contains about 70% of protein and all 2.5S RNA of the original nucleoprotein and retains about 50% of original activity. Amino acids Composition showed, that the protein is of alkaline nature and is rich in lysine. The alkaline nature of protein remains unchanged after trypsinolysis. On the basis of these studies it was assumed that the presence of firmly attached to the protein 2.5S RNA protects the branching enzyme against more powerful trypsinolysis and hinders loss of activity of the branching enzyme.

1,4-alpha-Glucan Branching Enzyme↗