Effects of protein phosphorylation with p43v-abl and protein kinase A catalytic subunit on fluorescence intensity.
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概要
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To study the effect of phosphorylation on protein conformation, a fluorescence spectroscopic study was performed on phosphorylated enolase and histoneHl proteins. The peak of fluorescence was 330 and 360 nm for each protein, respectively, when excited at 287 nm. The intensities of the fluorescence were measured during the phosphorylation reactions with the protein kinase A and p43<SUP>v-abl</SUP>, for serine, threonine and tyrosine, respectively. Slightly increased intensities at 330 and 360 nm for enolase and histoneH1 protein were observed by phosphorylation with p43<SUP>v-abl</SUP>, whereas decreased intensities occurred with the protein kinase A catalytic subunit. These data suggest that micro-structural changes are induced at the residue, either tyrosine, serine or threonine in the protein.
- 久留米大学医学部 The Kurume Medical Journal 編集部の論文
著者
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Yuge Kentaro
Department of Cardiology Regeneration&Advanced medical Science, Graduate School of Medicine, Gifu Un
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Ohtsu Yasushi
Department Of Virology Kurume University School Of Medicine
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Goto Masashi
Department Of Comprehensive Care And Education Tenri Hospital
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CHINAMI MASANOBU
Department of Gynecology and Obstetrics, Kurume University, School of Nedicine
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SHINGU MASAHISA
Department o f Microbiology, Kurume University School of Medicine
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