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Content available remote ATP-sensitive K+ transport in adrenal chromaffin granules
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EN
In the present study the influx of 86Rb+, a K+ analogue, was studied in mitochondria, microsomes and chromaffin granules prepared from adrenal gland medulla. The most active electrogenic 86Rb+ transport was found in the membrane fraction identified as chromaffin granules by marker enzyme estimation. The transport was found to be sensitive to ATP, ATPS, ADP and to the triazine dyes, but not to AMP and cAMP. The inhibition induced by ATP was observed in the absence of externally added Mg2+, suggesting that a free nucleotide, rather than the ATP-Mg complex, was required for inhibition. Furthermore, the 86Rb+ influx was found to be inhibited by Mg2+ alone, but not by Ca2+ and antidiabetic sulfonylureas. The 86Rb+ influx was not stimulated by potassium channel openers. In conclusion, our results indicate that an electrogenic, ATP-sensitive potassium transport system operates in the chromaffin granule membrane.
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Content available remote Isulfhydryl reagents with K+ transport in adrenal chromaffin granules
86%
EN
In the present study the functional role of SH groups in the Ca2+ -independent K+ selective channel activity in the membrane of bovine adrenal gland chromaffin granules has been studied. Ionic channel activity has been estimated using 86Rb+, a K+ analogue, flux measurements. The inhibition of chromaffin granules K+ channel by SH modifying agents, such as N ethylmaleimide, mersalyl and phenylarsenoxide, is described.
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