Inhibition of sodium transport in frog skin and iodination of tyrosine in vitro by a peptide of renal origin.
Eluates from a Sephadex G-25 column through which dog renal homogenate was passed contained a factor that inhibited lactoperoxidase (LPO)-catalyzed iodination of tyrosine as well as the short circuit current (active absorptive sodium flux) in isolated skin of the bullfrog (Rana catesbeiana). The active fraction also had a sulfhydryl-containing moiety, the concentration of which was correlated directly with the extent of inhibition of the LPO enzyme. The fractions active in inhibition of the LPO enzyme failed to affect the Na/K-AT-Pase enzyme. Whether the same moiety of the active fraction inhibits both the LPO enzyme and SCC in frog skin is unknown and awaits additional study.
D000818:Animals; D001692:Biological Transport; D002852:Chromatography, Ion Exchange; D004285:Dogs; D066298:In Vitro Techniques; D007668:Kidney / Q000032:analysis; D007784:Lactoperoxidase / Q000037:antagonists & inhibitors*; D007470:Monoiodotyrosine / Q000096:biosynthesis; D010455:Peptides / Q000494:pharmacology*; D010544:Peroxidases / Q000037:antagonists & inhibitors*; D011892:Rana catesbeiana; D012867:Skin / Q000378:metabolism*; D012964:Sodium / Q000378:metabolism*; D014443:Tyrosine / Q000378:metabolism*
D010455:Peptides; D014443:Tyrosine; D012964:Sodium; D007784:Lactoperoxidase; D010544:Peroxidases; D007470:Monoiodotyrosine