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- W1574201030 abstract "Abstract Salmon calcitonin (synthetic) was iodinated with the chloramine-T method and purified by gel filtration. The product was virtually free of uniodinated molecules as determined by enzymatic digestion and amino acid analysis. Greater than 80% of the incorporated iodine was in the form of monoiodotyrosine. The iodinated hormone bound specifically to renal and skeletal receptors and was indistinguishable from the uniodinated species by bioassays based on either the renal or skeletal action of calcitonin. The degradation of salmon 125I-calcitonin by renal plasma membranes was inhibited by agents that did not block the high affinity binding to receptors. Hormone bound to receptors remained biologically intact; after elution from receptors the hormone bound specifically to fresh membranes. High affinity, low capacity sites similar to those identified in renal plasma membranes were also found in membranes prepared from skeletal tissue; the apparent affinity constants were in the range of 1011 m-1 for each tissue. High affinity receptors for calcitonin were found in renal membrane preparations containing brush borders as well as preparations, presumably antiluminal in origin, that did not contain brush borders." @default.
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- W1574201030 date "1973-07-01" @default.
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- W1574201030 title "Renal Receptors for Calcitonin" @default.
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- W1574201030 doi "https://doi.org/10.1016/s0021-9258(19)43736-8" @default.
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