title: Structure of recombinant human carboxylesterase 1 isolated from whole cabbage looper larvae.
abstract: The use of whole insect larvae as a source of recombinant proteins offers a more cost-effective method of producing large quantities of human proteins than conventional cell-culture approaches. Human carboxylesterase 1 has been produced in and isolated from whole Trichoplusia ni larvae. The recombinant protein was crystallized and its structure was solved to 2.2 resolution. The results indicate that the larvae-produced enzyme is essentially identical to that isolated from cultured Sf21 cells, supporting the use of this expression system to produce recombinant enzymes for crystallization studies.
authors.affiliation: Department of Structural Biology, Weizmann Institute of Science, Rehovot 76100, Israel.
authors.forename: Harry M
authors.initials: HM
authors.lastname: Greenblatt
authors.forename: Tamara C
authors.initials: TC
authors.lastname: Otto
authors.forename: Melanie G
authors.initials: MG
authors.lastname: Kirkpatrick
authors.forename: Elena
authors.initials: E
authors.lastname: Kovaleva
authors.forename: Susan
authors.initials: S
authors.lastname: Brown
authors.forename: George
authors.initials: G
authors.lastname: Buchman
authors.forename: Douglas M
authors.initials: DM
authors.lastname: Cerasoli
authors.forename: Joel L
authors.initials: JL
authors.lastname: Sussman
mesh_terms: D000818:Animals; D043182:Carboxylesterase / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism; D002460:Cell Line; D006801:Humans; D006868:Hydrolysis; D007814:Larva / Q000235:genetics / Q000378:metabolism; D008958:Models, Molecular; D009036:Moths / Q000235:genetics / Q000378:metabolism; D020836:Protein Structure, Quaternary; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism
chemical_list: D011994:Recombinant Proteins; D043182:Carboxylesterase