Open AccessStructure of recombinant human carboxylesterase 1 isolated from whole cabbage looper larvae
Author(s) -
Greenblatt Harry M.,
Otto Tamara C.,
Kirkpatrick Melanie G.,
Kovaleva Elena,
Brown Susan,
Buchman George,
Cerasoli Douglas M.,
Sussman Joel L.
Publication year - 2012
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309112003326
Subject(s) - trichoplusia , carboxylesterase , recombinant dna , cabbage looper , biology , enzyme , larva , chinese hamster ovary cell , biochemistry , botany , gene , noctuidae , receptor
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 Å 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.