Properties and role of ferritin in the hemolymph of the chiton Clavarizona hirtosa

Kim, K.S., Webb, J. and Macey, D.J. (1986) Properties and role of ferritin in the hemolymph of the chiton Clavarizona hirtosa. Biochimica et Biophysica Acta (BBA) - General Subjects, 884 (3). pp. 387-394.

Abstract

The major iron-binding protein found in the hemolymph of the chiton Clavarizona hirtosa has been purified for the first time and identified as ferritin. This ferritin, which is present at a concentration of approx. 400 μg·ml−1, has a Mr of 28 000 and 25 500, exhibits microheterogeneity with isoelectric values in the range 5.3–6.0, binds 1500–2500 Fe atoms·mol−1 and is immunologically distinct from horse spleen ferritin. The initial rate of iron accumulation by ferritin molecules was determined to be markedly higher than that exhibited by horse spleen ferritin. Taken together, these data suggest that ferritin found in the hemolymph serves as a key component of the high-capacity transport system necessary to deliver iron to the rapidly mineralizing tissue of the radula in these molluscs.