Enzymatic and chemical deamination of 3-(beta-D-ribofuranosyl)adenine.

@article{Wolfenden1966EnzymaticAC,
  title={Enzymatic and chemical deamination of 3-(beta-D-ribofuranosyl)adenine.},
  author={Richard Wolfenden and Thomas K. Sharpless and I. S. Ragade and Nelson J. Leonard},
  journal={Journal of the American Chemical Society},
  year={1966},
  volume={88 1},
  pages={
          185-6
        }
}

Ribocation transition state capture and rebound in human purine nucleoside phosphorylase.

Kinetics of Phosphorolysis of 3-(β-d-Ribofuranosyl)Adenine and 3-(β-d-Ribofuranosyl)Hypoxanthine, Non-Conventional Substrates of Purine-Nucleoside Phosphorylase

Two well-characterized inhibitors of calf spleen PNP and E. coli PNP were found to inhibit phosphorolysis of RibfAde and RibfHyp with the same inhibition constants as for Ino, which indicates that phosphorlysis of 3-β-nucleosides occurs at the same active site as for the natural substrate Ino.

Groundworks for an evolutionary biochemistry: the iron-sulphur world.

The purine‐2‐deoxyribonucleosidase from Crithidia luculiae

The purine-2′-deoxyribonucleosidase was purified to homogeneity by a six-step procedure involving (NH4)2SO4 fractionation and chromatography on DEAE-cellulose, hydroxyapatite, Sephadex G-75, and a chromatofocusing resin.

Adenylates: Bound and unbound

An evaluation is made of the use of adenylate analogs as spatial, dimensional, and fluorescent probes of enzyme‐coenzyme binding sites.