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한국식물학회 / v.39, no.3, 1996년, pp.173-177 
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( Purification and Characterization of a Novel 21 kD Calcium Binding Protein from Dunaliella salina ) |
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| 초 록 |
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| A novel calcium binding protein (CaBP) was purified to electrophoretic homogeneity from Dunaliella salina. In the course of purification experiment, this CaBP was identified as a monomer and its molecular weight was about 21 kDand isoelectric point (pI) value was about 4.1 using isoelectrofocusing. This CaBP was able to bind Ca2+ even in the pressence of an excess MgCl2 and KCI both in solution. In the SDS-PAGE, the Ca2+-bound form was slower than the Ca2+-free form in the nondenaturing PAGE. This means that the CaBP undergoes conformational change in the Ca2+-bound condition. Furthermore, UV absorption spectrum and fluorescence intensity of this CaBP was investigated. UV absorption peak was appeared at about 258 nm and decreased somewhat in Ca2+-bound condition. In the measurement of fluorescence, maximum intensity was appeared at 303 nm and decreased in Ca2+-bound state, similarly as UV absorption spectrum. These show distinct changes upon Ca2+-binding, which indicate of structural and/or dynamic changes largely reminiscent of other members of the EF-hand Ca2+-binding protein family. |
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| 키워드 |
| Dunaliella salina;Calcium;Calcium-binding protein; |
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Journal of Plant Biology / v.39, no.3, 1996년, pp.173-177
한국식물학회
ISSN : 1226-9239
UCI : G100:I100-KOI(KISTI1.1003/JNL.JAKO199611920118033)
언어 : 영어 |
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| 논문 제공 : KISTI 한국과학기술정보연구원 |
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