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한국식물학회 / v.36, no.2, 1993년, pp.171-176 
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대두 유식물에서 Protein Kinase C의 부분 정제
( Partial Purification of Protein Kinase C in Glycine max ) |
| 최윤희; 이화여자대학교 생물과학과;
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| 초 록 |
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| Protein kinase C, a protein related in PI cascade, was partially purified from the cytosol protein of etiolated plants of Glycine max by DEAE-52 cellulose chromatography and phenylsepharose chromatography. When the DEAE column was eluted with 0-0.8 M linear gradient KCl, tow fractions were found that increased the phosphorylation of histon H1 about five and nine-fold in the presence of 5 $mu extrm{g}$/mL phosphatidylserine and 0.5 $mu extrm{g}$/mL diolein, respectively. These fractions were used as DEAE pool. The reaction eluted with relatively high concentration of KCl was loaded on phyenylsepharose column with 5 mM CaCl2 and eluted with 1 mM EGTA. A fraction contained the protein kinase C, which increased the phosphorylation of the histon H1 was fractionated. To determine the molecular weight of PKC, the fraction eluted from phenylsepharose column was analyzed by 5~15% polyacrylamide gel electrophoresis after concentrated with the Amicon membrane (YM10). That revealed two bands corresponding to 60 and 65 kGy by silver staining of the gel, respectively. |
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| 키워드 |
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Journal of Plant Biology / v.36, no.2, 1993년, pp.171-176
한국식물학회
ISSN : 1226-9239
UCI : G100:I100-KOI(KISTI1.1003/JNL.JAKO199311920116509)
언어 : 한국어 |
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| 논문 제공 : KISTI 한국과학기술정보연구원 |
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