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• W194446952 abstract "The properties, chemical nature, and applications of the RNases of taka-diastase are discussed in this chapter. As it was found in the preliminary experiments that taka-diastase contains at least three enzymes attacking RNA, research was begun, by studying the enzymatic properties of the major component. The study on the substrate specificity of the enzyme led to the unexpected discovery that, unlike pancreatic RNase, it splits phosphodiester bonds of 3'-guanylic acid in RNA. One of the minor components was found to split preferentially the phosphodiester bonds of 3'-adenylic acid in RNA. Since then the RNases in taka-diastase have become of interest in connection with the studies on the structure of RKA, no less important than the initial objective, the elucidation of the chemical nature of the enzymes. Several properties of ribonucleases in taka-diastase, such as pH optimum and enzyme activity, stability, and factor affecting activity, are discussed in this chapter. RNase T1 and RNase T2 can hydrolyze neither DNA nor bis-pnitrophenyl phosphate. For this reason, they are classified as ribonucleases rather than as nonspecific phosphodiesterases. Several applications, such as (a) applications in preparative chemistry, (b) application to the nucleotide distribution analysis in RNA, and (c) other possible applications are also discussed in this chapter." @default.
• W194446952 created "2016-06-24" @default.
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• W194446952 date "1964-01-01" @default.
• W194446952 modified "2023-10-17" @default.
• W194446952 title "Ribonucleases in Taka-Diastase: Properties, Chemical Nature, and Applications" @default.
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• W194446952 doi "https://doi.org/10.1016/s0079-6603(08)60739-4" @default.
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• W194446952 hasPublicationYear "1964" @default.
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