ISSN:
1432-0789
Keywords:
A bis-(p-nitrophenyl) phosphatase (BPNPase)
;
Forest soil extract
;
Fractionation on DEAE-cellulose column chromatography
;
Oligonucleotides
;
Cyclic nucleotides
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
,
Geosciences
,
Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
Notes:
Summary A bis-(p-nitrophenyl) phosphatase (BPN-Pase) was extracted from a forest soil and fractionated by DEAE-cellulose column chromatography into seven fractions (1, 2, 3, 4, 5, 6 and 7). The main fraction (fraction 5) was further fractionated into 3 subfraction (fractions 1, 2 and 3) by affinity chromatography for nuclease. The properties of the BPNPase in subfraction 3 were characterized and the results are reported in this article. Subfraction 3, which had a peak at about 278 run in the UV absorption spectrum, hydrolyzed 2′,3′-cyclic-nucleotides more readily than 3′,5′-cyclicnucleotides, adenylyl-(3′ → 5′)uridine, uridylyl-(3′ → 5′)adenosine, thymidine 3′-p-nitrophenyl phosphate, thymidine 5′-p-nitrophenyl phosphate, p-nitrophenyl phosphate and BPNP. Subfraction 3 hydrolyzed BPNP into 2 mol p-nitrophenyl and 1 mol inorganic phosphate during incubation. Apparent molecular weight of the BPNPase was estimated to be about 58 000 by gel filtration. The BPNPase activity had a pH optimum at 5.0 and was inhibited by Hg2+ and slightly inhibited by F− and PO 4 3− . These observations suggest that the BPNPase is subfraction 3 has been constituted mainly with 2′,3′cyclic-nucleotide 2′-phosphodiesterase [EC 3.1.4.16] or 2′,3′-cyclic-nucleotide 3′-phosphodiesterase [EC 3.1.4.37].
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF00255777
Permalink
