Protein Modification by ADP-ribose via Acid-labile Linkages (open access)

Protein Modification by ADP-ribose via Acid-labile Linkages

Article describing the preparation and chemical characterization of low molecular weight conjugates that were used as models for an acetal linkage between ADP-ribose and the hydroxyl group of a protein acceptor such as serine, threonine, tyrosine, hydroxyproline, or hydroxylysine residues. The amount of modification was approximately 16 pmol of ADP-ribose per mg of total protein, and proteins modified by acid-labile linkages were detected in all subcellular fractions examined, suggesting that the scope of this modification in vivo is broad.
Date: April 7, 1995
Creator: Cervantes-Laurean, Daniel; Loflin, Paul T.; Minter, David E.; Jacobson, Elaine L. & Jacobson, Myron K.
System: The UNT Digital Library
Characterization of the Nit6803 nitrilase homolog from the cyanotroph Pseudomonas fluorescens NCIMB 11764 (open access)

Characterization of the Nit6803 nitrilase homolog from the cyanotroph Pseudomonas fluorescens NCIMB 11764

This article reports the purification and characterization of a nitrilase (E.C. 3.5.5.1) (Nit11764) essential for the assimilation of cyanide as the sole nitrogen source by the cyanotroph, Pseudomonas fluorescens NCIMB 11764.
Date: January 16, 2021
Creator: Jones, Lauren B.; Wang, Xiaoqiang; Gullapalli, Jaya S. & Kunz, Daniel A.
System: The UNT Digital Library