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Sumi Kanij Rukshana Kim Soo Cheol Howlader Jewel Sharker Md Rajib Choi Kap Seong Choi Sang Ki Park Jong-In Nou Ill-Sup Kho Kang Hee 《Ocean Science Journal》2019,54(3):363-374
Ocean Science Journal - A carbonic anhydrase VII gene, encoding 277 amino acids, was identified in the intestinal tissue of pufferfish (Takifugu rubripes). The translated protein with an 833-bp... 相似文献
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Soo Cheol Kim Kanij Rukshana Sumi Jung Woo Kim Myeong Rak Choi Byung Hwa Min Kang Hee Kho 《Ocean Science Journal》2016,51(3):373-379
Carbonic anhydrase (CA), a ubiquitous enzyme found in many species, including fishes, is involved in physiological functions such as pH homeostasis, calcification, photosynthesis, and ionic regulation. CA I, a member of the α-CA family, is a cytoplasmic isozyme involved in carbon dioxide transport, ion exchange, and acid-base balance. Approximately half of the extant shark species occur only in deep waters; however, few published studies on sharks include these taxa. As fisheries worldwide enter deeper waters, the provision of biological data for these little-known taxa is critical to their management and conservation. To address this limitation, we aimed to detect CA I in various tissues of the shortspine spurdog (Squalus mitsukurii) and characterize its physicochemical properties by using sodium dodecyl-sulfate polyacrylamide gel electrophoresis and isoelectric focusing, together with immunohistochemistry. CA I was detected on SDS-PAGE and western blot analysis as a specific band at 29 kDa in various tissues of the shortspine spurdog, and as a specific band at pI 6.5 in various tissues of the shortspine spurdog by IEF and western blot analysis. CA I immunoreactivity in various tissues of the shortspine spurdog was detected in intracellular locations. To our knowledge, this is the first report of the localization of CA isozymes in various tissues of S. mitsukurii. 相似文献
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