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한국식물학회 / v.38, no.4, 1995년, pp.349-357 
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녹두의 하배축에서 분양한 Alkaline lnvertase의 정제와 특성
( Purification and Characterization of Alkaline Invertase from the Hypocotyls of Mung Bean (Phaseolus raiatus L.) ) |
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| 초 록 |
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| The alkaline invertase ($eta$-D-fructofuranoside fructohydrolase, EC 3.2.1.26) was isolated and characterized from the hypocotyls of mung bean (Phaseolus radiatus L.). The enzyme was purified by consecutive step using diethylaminoethyl (DEAE)-cellulose anion exchange, 1st Sephadex G-200, DEAE-Sephadex A50 and 2nd Sephadex G-200 chromatography. The overall purification was about 77-fold with a yield of about 6%. The finally purified enzyme exhibited a specific activity of about 48 $mu$mol of glucose produced mg-1 protein min-1 at pH 7.0 and appeared to be a single protein by nondenaturing polyacrylamide gel electrophoresis (PAGE). The enzyme had the native molecular weight of 450 kD and subunits molecular weight of 63 kD and 38 kD as estimated by Sephadex G-200 chromatography and SDS-PAGE, respectively, suggesting that the enzyme is a heteromultimeric protein composed of two types of subunits. On the other hand, the enzyme appeared to be not a glycoprotein according to the results of Con A chromatography and glycoprotein staining. The enzyme had a Km for sucrose of 19.7 mM at pH 7.0 and maximum activity around pH 7.5. The enzyme was most active with sucrose as substrate, compared to raffinose, cellobiose, maltose and lactose. These results indicate the alkaline invertase is a $eta$-fructofuranosidase. |
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| 키워드 |
| 정제;녹두;하배축;alkaline invertase;purification;mung vean;hypocotyls; |
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Journal of Plant Biology / v.38, no.4, 1995년, pp.349-357
한국식물학회
ISSN : 1226-9239
UCI : G100:I100-KOI(KISTI1.1003/JNL.JAKO199511920117477)
언어 : 영어 |
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| 논문 제공 : KISTI 한국과학기술정보연구원 |
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