Cloning, expression and characterization of horse L-ferritin in Escherichia coli.
Horse L-ferritin cDNA was cloned from horse liver, and the base sequence was determined. The L-ferritin was expressed using pTZ18U encoding lac promoter, and found to possess an additional 8-amino acid sequence at the N-terminus as compared with commercially obtained horse spleen (natural) ferritin. It was determined that there was Pro at position 94 in both the recombinant and natural L-ferritin, although it was previously reported that Leu was in this position in the natural species. Transmission electron microscopy showed that this recombinant ferritin formed a 24-mer shell.
Takeda
S
S
Protein Array Project, ERATO, JRDC, Tsukuba, Japan.
Ohta
M
M
Ebina
S
S
Nagayama
K
K
D000595:Amino Acid Sequence; D000818:Animals; D001052:Apoferritins / Q000648:ultrastructure; D001483:Base Sequence; D003001:Cloning, Molecular; D004247:DNA; D004926:Escherichia coli; D005293:Ferritins / Q000235:genetics* / Q000648:ultrastructure; D006736:Horses / Q000235:genetics*; D008099:Liver / Q000378:metabolism; D008854:Microscopy, Electron; D008969:Molecular Sequence Data
D004247:DNA; D005293:Ferritins; D001052:Apoferritins