Subunit Structure of Glucose Isomerase from Streptomyces griseofuscus, S-41
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概要
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The subunit structure of glucose isomerase isolated from Streptomyces griseofuscus, S-41 was studied using denaturants. The enzyme was quite stable to SDS under mild conditions, and dissociation into smaller subunits was dependent on pH and temperature. At acidic pH and high temperature, the enzyme showed rapid dissociation and inactivation. The dissociation into constituent subunits paralleled the loss of enzymatic activity. The enzyme was also dissociated into subunits by 6m guanidine hydrochloride. A single symmetrical elution peak was observed in Sepharose 6B column chromatography in the presence of 6 m guanidine hydrochloride, and the eluate showed no activity. Molecular weight estimations of the subunit, using both SDS polyacrylamide gel electrophoresis and gel nitration, were the same (43, 000). The N-terminal amino acid was identified as serine, and the yield of serine was estimated to be 43 percent from analyses of PTH and DNP derivatives. The sequence from N-terminal to the third amino acid was found to be Ser-Asp-Gin•••. Considering the molecular weight of the native enzyme as 180, 000 and the results obtained in the experiments here, it was concluded that native glucose isomerase was composedof four identical or very similar subunits with equal molecular weights and dimensions. The amounts of total and free thiols in the enzyme were estimated to be 6 mol and 2 mol, respectively, per mol of enzymeusing the titration method with DTNB. It was therefore considered that the enzyme contains two disulfide linkages.
- 社団法人 日本農芸化学会の論文
著者
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KASUMI Takafumi
National Food Research Institute
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Tsumura Nobuzo
National Food Research Institute Ministry Of Agriculture Forestry And Fisheries:(present Office)taiy
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Hayashi Kiyoshi
National Food Research Institute
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KASUMI Takafumi
National Food Research Institute, Ministry of Agriculture, Forestry and Fisheries
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