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Its first reports, published in 1977 by Davis and Abuchowski, described the covalent attachment of polyethylene glycol (PEG) to bovine serum albumin and liver catalase to reduce immunogenicity and prolong circulation time.[2,3] The primary goal was to create stealth therapeutics by shielding proteins from immune recognition and enzymatic degradation, and hence improving pharmacokinetics of therapeutic proteins, a principle later extended to drug delivery carriers such as liposomes, nanoparticles and peptides.[4] Advantages of Peptide Pegylation Shielding and stability : Polyethylene glycol increases the apparent molecular size of the peptide and reduces exposure of the core sequence to the surrounding biological environment, thereby shielding them from immune recognition and enzymatic degradation

60/008,316, filed December 7, 1995 (entitled Combinatorial Enzyme Development)

In addition to MHC-I binding, two functionally different Ly49Q motifs, the ITIM and the CRAC motif, play critical roles in phagocytosis

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GSH degradation occurs extracellularly, with -glutamyl transferase cleaving the -bond in GSH, GSSG, and conjugates, releasing Cys, forming -glutamyl amino acids and cysteinylglycine (CG)

Footnotes 1.^ References 1 AbriouelH.HerrmannA.StarkeJ.YousifN