K. Watanabe et al., Biochemical properties of canine serum ferritin: iron content and nonbinding to concanavalin A, BIOMETALS, 13(4), 2000, pp. 319-324
A sandwich enzyme-linked immunosorbent assay using H-subunit-rich canine he
art ferritin as a standard has been developed for measuring canine serum fe
rritin which is H-subunit-rich. Serum ferritin concentrations in 51 normal
dogs ranged from 143 to 1766 ng ml(-1), with a mean value of 479 +/- 286 (S
D) ng ml(-1). Serum ferritin iron concentrations as determined by an immuno
precipitation technique ranged from 30.4 to 115.9 ng ml(-1) in 15 normal do
gs with serum ferritin protein levels of 298 to 959 ng ml(-1). There was a
significant linear correlation between the serum ferritin iron and protein
levels (r=0.9441, P <0.001), and the mean iron/protein ratio of serum ferri
tin was 0.112 +/-0.017. When canine sera were incubated with concanavalin A
-Sepharose 4B, we observed the apparent binding of serum ferritin to concan
avalin A. However, ferritin obtained by heat-treating the sera at pH 4.8 to
remove the ferritin-binding proteins did not bind to the lectin. These res
ults suggest that canine serum ferritin contains a considerable amount of i
ron but no concanavalin A-binding G subunit present in human serum ferritin
.