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한국식물학회 / v.41, no.1, 1998년, pp.59-63 
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( Characterization of Small GTP-Binding Proteins in Plant Cell ) |
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| 초 록 |
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| To identify and characterize small GTP-binding proteins in plant cells, GTP-binding studies were performed with electroblotted plant proteins following SDS-polyacrylamide gel electrophoresis using [$alpha$-32P]GTP. Three speices of small GTP-binding protein (21, 23, and 27 kD) which have a specific GTP-binding property were identified in the membrane and cytosolic fractions of both monocotyledons (Zea mays) and dicotyledons (Glycine max). Moreover, these three species of small GTP-binding protein were gradually decreased when membranes were treated with hydroxylamine. This result indicates that these small GTP-binding proteins in plant cells are fatty acylated to the membrane lipids. The 27 kDa component was partially purified form hypocotyl membranes of Glycine max, following S-300 gel filtration, phenylsepharose CL-4B, hydroxyapatitie, and Q-sepharose column chromatography. This 27 kD protein was found to have both GTP-binding and GTPase activities. |
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| 키워드 |
| small G-prorein;fatty acylation;GTPase; |
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Journal of Plant Biology / v.41, no.1, 1998년, pp.59-63
한국식물학회
ISSN : 1226-9239
UCI : G100:I100-KOI(KISTI1.1003/JNL.JAKO199811920120019)
언어 : 영어 |
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| 논문 제공 : KISTI 한국과학기술정보연구원 |
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