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Structure of recombinant human carboxylesterase 1 isolated from whole cabbage looper larvae.
Greenblatt, Harry M; Otto, Tamara C; Kirkpatrick, Melanie G; Kovaleva, Elena; Brown, Susan; Buchman, George; Cerasoli, Douglas M; Sussman, Joel L.
Affiliation
  • Greenblatt HM; Department of Structural Biology, Weizmann Institute of Science, Rehovot 76100, Israel.
Article in En | MEDLINE | ID: mdl-22442219
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.
Subject(s)

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Carboxylesterase Limits: Animals / Humans Language: En Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun Year: 2012 Document type: Article Affiliation country: Israel

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Carboxylesterase Limits: Animals / Humans Language: En Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun Year: 2012 Document type: Article Affiliation country: Israel