Mh. Desmit et al., OPTIMIZED BACTERIAL PRODUCTION OF NONGLYCOSYLATED HUMAN TRANSFERRIN AND ITS HALF-MOLECULES, International journal of biochemistry & cell biology, 27(8), 1995, pp. 839-850
Transferrin is a glycoprotein functioning in iron transport in higher
eukaryotes, and consists of two highly homologous domains. To study th
e function of the glycan residues attached exclusively to the C-termin
al domain, we have constructed a plasmid allowing production of nongly
cosylated human transferrin in Escherichia coli. By molecular biologic
al and genetic techniques, production was stepped up to 60 mg/l. Simil
ar plasmids were constructed for production of the two half-transferri
ns. The recombinant proteins accumulate in inclusion-body-like aggrega
tes, where they appear to bind iron without causing bacteriostasis. Pr
oteins active in iron binding have been purified from these inclusion
bodies.