Richard Ling

Learn More
A general method for purification of any substrate of the ubiquitin pathway, the major eukaryotic proteolytic pathway, should utilize the common characteristic of covalent linkage of ubiquitin to substrate lysyl residues. The utility of a N-terminal histidine-tagged ubiquitin (HisUb) for in vivo conjugation and isolation of ubiquitinated proteins by metal(More)
The low abundance and heterogeneity of ubiquitinated proteins has led to the development and use of tagged forms of ubiquitin. Additional residues present at the ubiquitin amino terminus provide immunological and/or affinity sites to facilitate visualization, identification, and purification of ubiquitinated substrates by virtue of their covalent attachment(More)
The ubiquitin pathway targets proteins for degradation through the post-translational covalent attachment of the 76 amino acid protein ubiquitin to ∈-amino lysyl groups on substrate proteins. Two instability determinants recognized by the ubiquitin pathway in Saccharomyces cerevisiae have been identified. One is described by the N-end rule and requires(More)
Many methods for the determination of iodinated compounds in thyroid extracts by paper and thin-layer chromatography have been reported. Some of them do not separate inorganic iodide (l-3)) diiodothyronine (4-8)) or monoand di-iodotyrosines (6, 9). Others use more than one solvent system (4, 7, lO-12), usually one system for iodotyrosines and another for(More)
the host thyroid. The tumors themselves showed extremely low incorporation, although thyroidectomy of the host significantly increased the incorporation in the tumors. However, results of incorporation experiments do not distinguish the transitional from the autonomous tumors. Tumor growth also caused iodide peroxidase activity in the host thyroid to(More)
  • 1