Abstract:
:The use of tobacco plants as a novel expression system for the production of human homotrimeric collagen I is presented in this report. Constructs were engineered from cDNA encoding the human proalpha1(I) chain to generate transgenic tobacco plants expressing collagen I. The recombinant proalpha1(I) chains were expressed as disulfide-bonded trimers and were shown to fold into a stable homotrimeric triple helix. Moreover, the recombinant procollagen was subsequently processed to collagen as it occurs in animals. Large amounts of recombinant collagen were purified from field grown plant material. The data suggest that plants are a valuable alternative for the recombinant production of collagen for various medical and scientific purposes.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Ruggiero F,Exposito JY,Bournat P,Gruber V,Perret S,Comte J,Olagnier B,Garrone R,Theisen Mdoi
10.1016/s0014-5793(00)01259-xkeywords:
subject
Has Abstractpub_date
2000-03-03 00:00:00pages
132-6issue
1eissn
0014-5793issn
1873-3468pii
S0014-5793(00)01259-Xjournal_volume
469pub_type
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