ChemInform Abstract: SYNTHETIC STUDIES ON PHOSPHORYLATING REAGENT PART 4, A NOVEL SYNTHESIS OF NUCLEOSIDE-3′,5′-CYCLIC PHOSPHATES BY THE USE OF 2-(N,N-DIMETHYLAMINO)-4-NITROPHENYL PHOSPHATE

1975 ◽  
Vol 6 (32) ◽  
pp. no-no
Author(s):  
YOSHIHIKO TAGUCHI ◽  
YOSHITAKA MUSHIKA
1959 ◽  
Vol 37 (8) ◽  
pp. 945-952 ◽  
Author(s):  
Neil Tomlinson

A nuclease from muscle of lingcod (Ophiodon elongatus) has been purified by chromatography on diethylaminoethyl cellulose in the free-base form by stepwise elution with increasing concentrations of tris(hydroxymethyl)aminomethane. HCl, pH 7.0. The nuclease has been shown to hydrolyze ribonucleic acid, adenosine 3′-benzyl phosphate, thymidine 3′-p-nitrophenyl phosphate, and thymidine 5′-p-nitrophenyl phosphate. The latter compound was hydrolyzed at a very low rate. It did not hydrolyze adenosine 2′- or 5′- benzyl phosphate or certain nucleoside cyclic phosphates. The enzyme was inhibited by monoiodoacetate but not by heparin.


1959 ◽  
Vol 37 (1) ◽  
pp. 945-952 ◽  
Author(s):  
Neil Tomlinson

A nuclease from muscle of lingcod (Ophiodon elongatus) has been purified by chromatography on diethylaminoethyl cellulose in the free-base form by stepwise elution with increasing concentrations of tris(hydroxymethyl)aminomethane. HCl, pH 7.0. The nuclease has been shown to hydrolyze ribonucleic acid, adenosine 3′-benzyl phosphate, thymidine 3′-p-nitrophenyl phosphate, and thymidine 5′-p-nitrophenyl phosphate. The latter compound was hydrolyzed at a very low rate. It did not hydrolyze adenosine 2′- or 5′- benzyl phosphate or certain nucleoside cyclic phosphates. The enzyme was inhibited by monoiodoacetate but not by heparin.


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