Purification and characterization of a guanosine diphosphatase activity from calf liver microsomal salt wash proteins.

@article{Raychaudhuri1985PurificationAC,
  title={Purification and characterization of a guanosine diphosphatase activity from calf liver microsomal salt wash proteins.},
  author={P. Raychaudhuri and S. Ghosh and U. Maitra},
  journal={The Journal of biological chemistry},
  year={1985},
  volume={260 14},
  pages={
          8306-11
        }
}
A potent guanosine diphosphatase activity that hydrolyzes GDP to 5'-GMP + Pi has been isolated and purified from the salt wash proteins of calf liver microsomes. The purified enzyme, a monomeric protein of approximate Mr 46,000, possesses nucleotide substrate specificity since, among the nucleoside diphosphates and triphosphates tested, only GDP and UDP are hydrolyzed by the enzyme. The relative affinity of the enzyme for GDP is, however, much higher than for UDP. The effect of the enzyme on… Expand
Glycoprotein reglucosylation and nucleotide sugar utilization in the secretory pathway: identification of a nucleoside diphosphatase in the endoplasmic reticulum
TLDR
By eliminating UDP, which is an inhibitory product of the UDP‐Glc:glycoprotein glucosyltransferase, it is likely to promote reglucosylation reactions involved in glycoprotein folding and quality control in the ER. Expand
Enzyme nomenclature. Recommendations 1984. Supplement 2: corrections and additions.
  • E. Webb
  • Art, Medicine
  • European journal of biochemistry
  • 1989
This document contains 275 entries for new enzymes which have come to light since the finalization of the 1984 edition at the end of November, 1983, and the publication of Supplement 1 (Eur. J.Expand