PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 20005217-1 2010 We have shown previously that conjugation of polyethylene glycol (PEG) chains to recombinant human acetylcholinesterase (rHuAChE) results in the extension of its residence time in the circulation of mice and monkeys [1,2]. Polyethylene Glycols 45-64 acetylcholinesterase (Cartwright blood group) Homo sapiens 99-119 20005217-1 2010 We have shown previously that conjugation of polyethylene glycol (PEG) chains to recombinant human acetylcholinesterase (rHuAChE) results in the extension of its residence time in the circulation of mice and monkeys [1,2]. Polyethylene Glycols 66-69 acetylcholinesterase (Cartwright blood group) Homo sapiens 99-119 20005217-2 2010 By profiling the pharmacokinetic behavior of an array of well-defined hypolysine human mutant AChE molecules following PEGylation, we now determine that the duration of these enzyme forms in the circulation of rhesus macaques correlates with their number of appended PEG moieties, and is influenced by the actual location of the PEG chains at the molecule surface, as well. Polyethylene Glycols 119-122 acetylcholinesterase (Cartwright blood group) Homo sapiens 94-98 20005217-2 2010 By profiling the pharmacokinetic behavior of an array of well-defined hypolysine human mutant AChE molecules following PEGylation, we now determine that the duration of these enzyme forms in the circulation of rhesus macaques correlates with their number of appended PEG moieties, and is influenced by the actual location of the PEG chains at the molecule surface, as well. Polyethylene Glycols 267-270 acetylcholinesterase (Cartwright blood group) Homo sapiens 94-98 20005217-5 2010 Thus, an inverse relationship between anti-AChE antibody production and PEG loading was observed following repeated administration of the different PEGylated hypolysine human AChEs to mice. Polyethylene Glycols 72-75 acetylcholinesterase (Cartwright blood group) Homo sapiens 43-47