A. Hoshino et al., COMPLETE SEQUENCE-ANALYSIS OF RAT TRANSFERRIN AND EXPRESSION OF TRANSFERRIN BUT NOT LACTOFERRIN IN THE DIGESTIVE GLANDS, Comparative biochemistry and physiology. B. Comparative biochemistry, 113(3), 1996, pp. 491-497
Rat milk and digestive juices contain transferrin but not lactoferrin,
which is a major iron-binding protein in these secretions of human an
d mouse. To compare the structure of rat transferrin to that of transf
errins and lactoferrins in other species, we isolated a cDNA clone con
taining the entire coding region of transferrin from rat liver and det
ermined its sequence. The amino-acid. sequence of rat transferrin had
69.8% identity with that of human transferrin and 48.8% identity with
that of human lactoferrin. Rat transferrin, like other transferrins, h
ad the potential N-linked glycosylation site only in the C-terminal do
main, although lactoferrins characterized so far contained the glycosy
lation sites in both the N- and C-terminal domains. Southern and North
ern analyses showed that there was the gene specifically hybridized wi
th the mouse lactoferrin cDNA in rat genomic DNA, but only the transfe
rrin mRNA was detected in mammary gland, submaxillary gland and pancre
as oi rat. These results suggest that the rat lactoferrin gene is sile
nt in the mammary gland, and transferrin can serve as a functional sub
stitute for lactoferrin in rat.