Acid phosphatases and ribonucleases from Dactylis glomerata seeds. I. Chromatographic and electrophoretic heterogeneity of the enzymes | Zendy

E. Wieczorek | Zendy; Janina Wiśniewska | Zendy; B Morawiecka | Zendy

Open Access

Acid phosphatases and ribonucleases from Dactylis glomerata seeds. I. Chromatographic and electrophoretic heterogeneity of the enzymes

Author(s) -

E. Wieczorek,

Janina Wiśniewska,

B Morawiecka

Publication year - 2015

Publication title -

acta societatis botanicorum poloniae

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.297

H-Index - 29

eISSN - 2083-9480

pISSN - 0001-6977

DOI - 10.5586/asbp.1978.040

Subject(s) - ribonuclease , chemistry , thermolabile , phosphatase , sephadex , enzyme , acid phosphatase , cellulose , chromatography , biochemistry , rna , gene

Acid phosphatase and ribonuclease extracted with 0.1 M sodium acetate buffer, pH 5.1 from Dactylis glomerata seeds, and partially purified by means of 70% ethanol precipitation showed electrophoretic and Chromatographic heterogeneity. After chromatography on DEAE-cellulose acid phosphatase and ribonuclease were separated into four peaks. Nonadsorbing acid phosphatase on DEAE-cellulose (peak I) was separated into four peaks on CM-cellulose. The highest activity (11 units/mg) was found in fraction b (acid phosphatase Ib). The enzyme was activated by Mg2+, Ca2+, Li+, Cs+, K+ ions and inhibited by Cu2+, Zu2+, F- and Mo-6 at optimum pH 5.0. Strong absorbing ribonuclease on DEAE-cellulose (peak IV) was further separated on G-200 Sephadex into two molecular forms: RN-asa1 and RN-ase2. Ribonuclease l, a thermolabile enzyme with specific activity 807 units/mg, showed an optimal activity at pH 4.8-5.1

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