Purification and characterization of two forms of maltotetraose-forming amylase from Pseudomonas stutzeri.
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- NAKADA Tetsuya
- Hayashibara Biochemical Laboratories, Inc.
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- KUBOTA Michio
- Hayashibara Biochemical Laboratories, Inc.
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- SAKAI Shuzo
- Hayashibara Biochemical Laboratories, Inc.
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- TSUJISAKA Yoshio
- Hayashibara Biochemical Laboratories, Inc.
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説明
Pseudomonas stutzeri MO-19 produced two active forms of extracellular maltotetraose-forming amylase. Both forms, G4-l and G4-2, were purified to electrophoretic homogeneity. The molecular masses of G4-1 and G4-2 were 57 kd and 46 kd by SDS-polyacrylamide gel electrophoresis, respectively. An identical N-terminal sequence up to 20 amino acid residues and similar amino acid compositions were obtained from both forms, but different C-terminal amino acids, leucine from G4-1 and alanine from G4-2, were released by carboxypeptidase Y. By in vitro incubation with a culture supernatant containing protease activity, G4-1 was converted into G4-2 without any loss of the amylase activity. It was concluded that G4-2 was a product derived by the limited proteolysis of G4-1, and that the proteolysis occured in the C-terminal region of G4-1. G4-2 was more thermostable than G4-1, and had a 20-fold higher Michaelis constant value for glycogen, which was 50 mg/ml against 2.3 mg/ml of G4-1. G4-1 adsorbed onto raw starch granules while G4-2 did not.
収録刊行物
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- Agricultural and Biological Chemistry
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Agricultural and Biological Chemistry 54 (3), 737-743, 1990
公益社団法人 日本農芸化学会
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詳細情報 詳細情報について
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- CRID
- 1390001206463969920
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- NII論文ID
- 110006324833
- 10012491010
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- NII書誌ID
- AA00515312
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- COI
- 1:CAS:528:DyaK3cXitFaru7g%3D
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- ISSN
- 18811280
- 00021369
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- PubMed
- 1368535
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- 本文言語コード
- en
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- 資料種別
- journal article
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- データソース種別
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- JaLC
- Crossref
- PubMed
- CiNii Articles
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- 使用不可