Tissue transglutaminase (TGase) is a Ca(2+)-dependent enzyme that catalyzes cross-linking of intracellular proteins through a mechanism that involves isopeptide bond formation between Gln and Lys residues. In addition to its transamidation activity, TGase can bind guanosine 5'-triphosphate (GTP) and does
International journal of pharmaceutics, 397(1-2), 179-183 (2010-07-06)
A novel nucleic acid compaction device based on a positively-charged alpha,epsilon-poly-l-lysine was realized for the first time. The polycationic peptide was obtained by assembling Fmoc and Boc orthogonally protected l-lysine monomers by solid phase synthesis. The route to the novel
Biochimica et biophysica acta, 1620(1-3), 235-244 (2003-02-22)
Proteins are subject of posttranslational modification by sugars and their degradation products in vivo. The process is often referred as glycation. L-Dehydroascorbic acid (DHA), an oxidation product of L-ascorbic acid (vitamin C), is known as a potent glycation agent. A
Biochemical and biophysical research communications, 371(4), 818-822 (2008-05-13)
We report a method for site-specifically incorporating l-lysine derivatives into proteins in mammalian cells, based on the expression of the pyrrolysyl-tRNA synthetase (PylRS)-tRNA(Pyl) pair from Methanosarcina mazei. Different types of external promoters were tested for the expression of tRNA(Pyl) in
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