Full TGIF Record # 5624
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Author(s):Lorenc-Kubis, I.; Morawiecka, B.
Author Affiliation:Zaklad Biochemii Molekularnej, Instytut Biochemii, Uniwersytet Wroclaw, Wroclaw, Poland
Title:Preliminary studies on ribonucleases from Poa pratensis seeds
Source:Acta Societatis Botanicorum Polaniae. Vol. 43, No. 4, 1974, p. 471-478.
Keywords:TIC Keywords: Poa pratensis; Enzymes; pH; Temperatures; EDTA; Ribonuclease
Geographic Terms:Poland
Abstract/Contents:Ribonuclease was extracted from Poa pratensis seeds with 0.1M acetate buffer of pH 5.1 and then precipitated with alcohol. The enzyme was separated into 5 fractions (I-V) by chromatography on DEAE cellulose at pH 5.1. The enzyme was stable at 60 deg C at pH 7.1 but adjustment of pH to 5.1 or 8.7 caused a decrease of enzymatic activity at temperatures )50 and 40 deg , respectively. Optimum pH for ribonucleases I-III and V was 7.1-7.3 and that for IV was 8.1. All the enzymes were inhibited by Ca2+ and EDTA, whereas Mg2+ inhibited II-IV but not I and V. Ribonucleases IV and V showed only one activity band in disk electrophoresis, whereas I-III were heterogeneous.
Language:English
References:18
Note:Summary appears in Polish
ASA/CSSA/SSSA Citation (Crop Science-Like - may be incomplete):
Lorenc-Kubis, I., and B. Morawiecka. 1974. Preliminary studies on ribonucleases from Poa pratensis seeds. Acta Societatis Botanicorum Polaniae. 43(4):p. 471-478.
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