Functional expression and production of human H-ferritin in Pichia pastoris.
Human heavy chain ferritin (H-ferritin) was cloned from human heart cDNA library and expressed in Pichia pastoris. The H-ferritin transformant was cultivated by fed-batch and the cell mass reached about 52 g cell dry wt l(-1) after 150 h. In atomic absorption spectrometry analysis, intracellular content of iron in H-ferritin transformant was measured to 3038 +/- 72 microg g(-1) which was 9.6-fold more than that of control strain.
Lee
Jung-Lim
JL
College of Life Sciences, Kyung Hee University, Suwon 449-701, Korea.
Song
Hyung-Seok
HS
Kim
Hyun-Joong
HJ
Park
Jong-Hwan
JH
Chung
Dae-Kyun
DK
Park
Cheon-Seok
CS
Jeoung
Dooil
D
Kim
Hae-Yeong
HY
D003001:Cloning, Molecular; D005293:Ferritins / Q000096:biosynthesis* / Q000737:chemistry / Q000235:genetics* / Q000302:isolation & purification; D015966:Gene Expression Regulation, Fungal; D006801:Humans; D007501:Iron / Q000032:analysis; D010843:Pichia / Q000235:genetics* / Q000254:growth & development / Q000302:isolation & purification / Q000378:metabolism*; D011786:Quality Control; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000235:genetics
D011994:Recombinant Proteins; D005293:Ferritins; D007501:Iron