Russian Journal of Biological Physics and Chemisrty Russian Journal of Biological Physics and Chemisrty АКТУАЛЬНЫЕ ВОПРОСЫ БИОЛОГИЧЕСКОЙ ФИЗИКИ И ХИМИИ 2499-9962 54148 МОЛЕКУЛЯРНАЯ БИОФИЗИКА И ФИЗИКА БИОМОЛЕКУЛ MOLECULAR BIOPHYSICS AND PHYSICS OF BIOMOLECULES МОЛЕКУЛЯРНАЯ БИОФИЗИКА И ФИЗИКА БИОМОЛЕКУЛ Properties of the ion transporting protein isolated from rat liver microsomes Свойства ион-транспортирующего белка, выделенного из микросом печени крысы Таланов Е Ю Talanov E Iu evg-talanov@yandex.ru Мосенцов А А Mosentsov A A Миронова Г Д Mironova G D Институт теоретической и экспериментальной биофизики РАН ru Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences ru Харьковский национальный университет им. В.Н. Каразина ru V.N. Karazin Kharkiv National University ru Институт теоретической и экспериментальной биофизики РАН ru Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences ru 25 06 2017 25 06 2017 2 1 189 193 20 06 2017 20 06 2017 https://rusjbpc.ru/en/nauka/article/54148/view

В настоящей работе с помощью метода водно-этанольной экстракции из микросом печени крысы выделен и очищен ион-транспортирующий белок-канал. Изучены его электрофизиологические и регуляторные свойства. Показано, что минимальная величина канала составляет 10pS. При реконструкции в БЛМ данного белка, формируются каналы с многоуровневой проводимостью. Проводимость данного белка может распадаться на различные уровни. Величина проводимости кластеров кратна величине проводимости одиночного белка - канала. Вольтамперная характеристика (ВАХ) полученная в диапазоне напряжения от -100 mV до 100 mV свидетельствует о потенциал - чувствительности обнаруженного микросомального белка-канала. Полученные данные свидетельствуют о том, что белок выделенный из микросом не является селективным по К+, что возможно связанно с местом его локализации и его участии в процессах опосредованных не только транспортом калия но и других одновалентных ионов. Обнаруженные эффекты ATP и ADP на выделенный из микросом гепатоцитов крысы канал, позволяют относить его к семейству АТP-чувствительных белков. Ингибирование изучаемого белка-канала 5-ГД, указывает на то, что митоКАТP подобные белки, помимо митохондрий могут быть локализованы и в эндоплазматическом ретикулуме.

In this work, an ion transporting channel protein has been isolated and purified from the rat liver microsomes by using the water-ethanol extraction method. The electrophysiological and regulatory properties of the protein were studied. It was shown that the minimum conductance value of the channel is 10pS. When reconstructed into the BLM, the protein formed ion channels with a multilevel conductance. The conductance of this channel protein is divided into different levels. The conductance value of clusters is a multiple of that of the single protein channel. Volt-ampere characteristics (VAC) recorded in the voltage range from -100mV to 100mV indicates the potential-sensitivity of the microsomal channel protein. The data obtained suggest that the protein isolated from microsomes is not selective for K+ ions, which may be due to its localization and its participation in processes mediated by transport of not only potassium, but also other monovalent ions. The observed effects of ATP and ADP on activity of the channel isolated from microsomes of rat hepatocytes make it possible to classify it as a member of ATP-sensitive protein family. The inhibitory effect of 5-hydroxydecanoate on the studied channel protein indicates that mitoKATP like proteins, in addition to mitochondria, can also be localized in the endoplasmic reticulum.

 митохондрии микросомы БЛМ КАТР-каналы 5- ГД mitochondria microsomes black lipid membranes ATP-dependent potassium channels 5-hydroxydecanoate

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