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. 1993 Aug 19;1174(2):218-20.
doi: 10.1016/0167-4781(93)90121-s.

Cloning, expression and characterization of horse L-ferritin in Escherichia coli

S Takeda  1 , M Ohta, S Ebina, K Nagayama
Affiliations

Cloning, expression and characterization of horse L-ferritin in Escherichia coli

S Takeda et al. Biochim Biophys Acta. .

Abstract

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.

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