Abstract
Artery-to-vein and artery-to-urine transit characteristics of 125I-myoglobin across the rabbit kidney were compared to those of Cd-metallothionein (CdMT) labeled with 109Cd, and their interaction during tubular reabsorption was determined. Both proteins are reabsorbed by a saturable system, mutually inhibit each other''s reabsorption and suffer similar tubular transit delays. Since myoglobin inhibition of CdMT reabsorption is fully reversible, the 2 proteins may compete for reabsorption by a common transport system. This system also reacts with hemoglobin, indicating that its affinity for substrates is determined by factors other than purely size of the protein molecule.

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