PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 25244429-3 2015 At the same time, the hydrazide on TGH reacts with the aldehyde on poly(ethylene glycol) (PEG) and forms a hydrazone bond. Polyethylene Glycols 67-88 carboxylesterase 1 Homo sapiens 35-38 1418688-4 1992 PEG-modified CEH synthesized various cholesterol esters with significant substrate specificity. Polyethylene Glycols 0-3 carboxylesterase 1 Homo sapiens 13-16 25244429-0 2015 Preparation of pH-stimuli-responsive PEG-TGA/TGH-capped CdTe QDs and their application in cell labeling. Polyethylene Glycols 37-40 carboxylesterase 1 Homo sapiens 45-48 1418688-1 1992 The solvent dependency and substrate specificity of polyethylene glycol (PEG)-modified cholesterol esterase (CEH) catalyzing cholesterol ester synthesis in organic solvents were studied. Polyethylene Glycols 52-71 carboxylesterase 1 Homo sapiens 109-112 1418688-1 1992 The solvent dependency and substrate specificity of polyethylene glycol (PEG)-modified cholesterol esterase (CEH) catalyzing cholesterol ester synthesis in organic solvents were studied. Polyethylene Glycols 73-76 carboxylesterase 1 Homo sapiens 109-112 1418688-2 1992 When cholesterol and linoleic acid were used as the substrates, PEG-modified CEH synthesized cholesterol linoleate only in water-immiscible organic solvents. Polyethylene Glycols 64-67 carboxylesterase 1 Homo sapiens 77-80 1418688-3 1992 Among some solvents capable of solubilizing all of the reaction components (PEG-modified CEH, cholesterol, and linoleic acid), chloroform was most suitable for enzymatic cholesterol linoleate synthesis, and the synthetic activity for cholesterol linoleate decreased in the order chloroform, benzene, toluene, and cyclohexane. Polyethylene Glycols 76-79 carboxylesterase 1 Homo sapiens 89-92 25244429-3 2015 At the same time, the hydrazide on TGH reacts with the aldehyde on poly(ethylene glycol) (PEG) and forms a hydrazone bond. Polyethylene Glycols 90-93 carboxylesterase 1 Homo sapiens 35-38