Structure of recombinant human carboxylesterase 1 isolated from whole cabbage looper larvae.
Acta Crystallogr Sect F Struct Biol Cryst Commun
; 68(Pt 3): 269-72, 2012 Mar 01.
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.
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