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家兎網狀赤血球의 核酸分解酵素의 精製와 그 性狀

Purification and Charaterization of Nucleases from Rabbit Reticulocytes

전남의대잡지 1968년 5권 2호 p.217 ~ 229
노광철,
소속 상세정보
노광철 (  ) - 전남대학교 의과대학 생화학교실

Abstract


Nucleases, an acid deoxyribonuclease (DNase) having an optimal pH 5.0 and alkaline ribonuclease(RNase)capable of hydrolyzing reticulocyte ribosomal RNA, were purified 3,000 and 150-fold, respectively, from rabbit reticulocytes by the same purification procedures simultaneously. Evidence is presented indicating that DNase and RNase associated with rabbit reticulocytes are distinct. enzyme entities.
The RNase was separated from DNase by chromatography on a Sephadex G-75 column, and showed a sharp pH optimum at pH 7.4. The RNase/DNase ratios differed at each step of purification procedures. In contrast, to heat-labile DNase, the RNase was heat-stable, being; not. completely inactivated even at 100° for 10 minutes at p117.4. Urea and ρ-chlormercuribenzoate which inhibited the RNase activated the RNase, urea being much more potent than ρ-chlormercuribenzoate. The DNase was completely inhibited by heparin at 90 μg/ ml concentration whereas the inhibition by heparin of RNase was inversely proportional to the heparin concentrations, the inhibition being most marked at 45 μg/ml but released, completely at 360 μg/ml concentration. The RNase activity was inhibited by Mg24 above 3 mM, 30 mM K+, and 1 mM ethylenediamine tetraacetate.
The increase in the percentages of recovery at some steps of the purification procedures for RNase as well as for DNase, and the activating effects of urea and p-chlormercuribenzoate on RNase suggested the occurrence of inhibitors for RNase and RNase in rabbit reticulocytes.

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