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The Kinetics of Serum and Tissue Ferritins: Relation to Carbohydrate Content
Author(s) -
Halliday J. W.,
Mack U.,
Powell L. W.
Publication year - 1979
Publication title -
british journal of haematology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.907
H-Index - 186
eISSN - 1365-2141
pISSN - 0007-1048
DOI - 10.1111/j.1365-2141.1979.tb01166.x
Subject(s) - ferritin , concanavalin a , half life , chemistry , clearance , sepharose , biochemistry , ultracentrifuge , microgram , carbohydrate , kinetics , mole , metabolism , blood proteins , endocrinology , medicine , biology , enzyme , pharmacokinetics , in vitro , physics , quantum mechanics , urology
S ummary . Significant differences were observed in the rate of disappearance from plasma of ferritins purified from rat serum and from different organs. Ferritin from all sources including purified serum ferritin was rapidly removed from plasma by the liver. No difference in biological half‐life was observed between apoferritin prepared by ultracentrifugation of liver ferritin and whole liver ferritin and ironloaded animals cleared injected serum ferritin from plasma at a comparable rate to normal rats. When amounts of 100 μg of ferritin were injected into rats the half‐life was significantly lengthened. The study confirmed the fact that ferritin iron and ferritin protein were removed from plasma at the same rate. No consistent effect of acidic or more basic isoferritin composition on biological half‐life was apparent. After chromatography on concanavalin A‐Sepharose 6B those ferritins which were predominantly bound to Con A‐Sepharose had a half‐life which was approximately twice that of ferritins which did not bind. It is concluded that the variation in plasma disappearance of ferritins of different tissue origin was explainable on the basis of carbohydrate content of the molecule.