The purification of a cysteine-dependent NAD+ glycohydrolase activity from bovine erythrocytes and evidence that it exhibits a novel ADP-ribosyltransferase activity
- 15 September 1995
- journal article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 310 (3) , 931-937
- https://doi.org/10.1042/bj3100931
Abstract
No abstract availableKeywords
This publication has 29 references indexed in Scilit:
- Glyceraldehyde‐3‐phosphate activates auto‐ADP‐ribosylation of glyceraldehyde‐3‐phosphate dehydrogenaseFEBS Letters, 1993
- Nitric oxide preferentially stimulates auto‐ADP‐ribosylation of glyceraldehyde‐3‐phosphate dehydrogenase compared to alcohol or lactate dehydrogenaseFEBS Letters, 1993
- Reversible ADP‐ribosylation of the 78 kDa glucose‐regulated proteinFEBS Letters, 1990
- Enzymic and nonenzymic mono ADP-ribosylation of proteins in skeletal muscleBiochemical and Biophysical Research Communications, 1989
- Thiol reagents are substrates for the ADP‐ribosyltransferase activity of pertussis toxinFEBS Letters, 1988
- Structure-activity analysis of the activation of pertussis toxinBiochemistry, 1987
- Regulation of endogenously catalyzed ADP-ribosylation in adipocyte plasma membranes by Ca2+ and calmodulinCell Calcium, 1985
- ADP‐ribosyltransferase from beef liver which ADP‐ribosylates elongation factor‐2FEBS Letters, 1984
- ADP-ribosylation of isolated rat islets of LangerhansBiochemical and Biophysical Research Communications, 1984
- Nicotinamide Adenine Dinucleotide Splitting Enzyme: A Characteristic of the Mouse MacrophageScience, 1978