Title : Toward PKU enzyme replacement therapy: PEGylation with activity retention for three forms of recombinant phenylalanine hydroxylase.

Pub. Date : 2004 Jan

PMID : 14741785






6 Functional Relationships(s)
Download
Sentence
Compound Name
Protein Name
Organism
1 Three recombinantly produced PAH enzymes were reacted with activated PEG species, with the aim of developing a stable and active PKU enzyme replacement. Polyethylene Glycols phenylalanine hydroxylase Homo sapiens
2 All PEG-derivatized PAH species retained catalytic activity, and, at low numbers of PEG molecules attached, these PEGylated PAH proteins were found to be more active and more stable than their non-derivatized PAH counterparts. Polyethylene Glycols phenylalanine hydroxylase Homo sapiens
3 All PEG-derivatized PAH species retained catalytic activity, and, at low numbers of PEG molecules attached, these PEGylated PAH proteins were found to be more active and more stable than their non-derivatized PAH counterparts. Polyethylene Glycols phenylalanine hydroxylase Homo sapiens
4 All PEG-derivatized PAH species retained catalytic activity, and, at low numbers of PEG molecules attached, these PEGylated PAH proteins were found to be more active and more stable than their non-derivatized PAH counterparts. Polyethylene Glycols phenylalanine hydroxylase Homo sapiens
5 All PEG-derivatized PAH species retained catalytic activity, and, at low numbers of PEG molecules attached, these PEGylated PAH proteins were found to be more active and more stable than their non-derivatized PAH counterparts. Polyethylene Glycols phenylalanine hydroxylase Homo sapiens
6 All PEG-derivatized PAH species retained catalytic activity, and, at low numbers of PEG molecules attached, these PEGylated PAH proteins were found to be more active and more stable than their non-derivatized PAH counterparts. Polyethylene Glycols phenylalanine hydroxylase Homo sapiens