Purification and Characterization of a Cysteine Proteinase Inhibitor(Cystatin) from Seeds of Foxtail Millet, Setaria italica.
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- TASHIRO Misao
- School of Human Environmental Sciences, Mukogawa Women's University
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- KURATA Akie
- Koka Women's Junior College
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- HASEGAWA Atsuko
- Biwako Research Institute, Otuka Foods Co., Ltd.
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- SAWADA Sayuri
- School of Human Environmental Sciences, Mukogawa Women's University
Bibliographic Information
- Other Title
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- アワ種子からのシステインプロテイナーゼインヒビターの精製と性質
- アワ シュシ カラ ノ システインプロテイナーゼインヒビタ ノ セイセイ ト セイシツ
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Abstract
A cysteine proteinase inhibitor was purified from the extract of seeds of foxtail millet, Setaria italica, to an electrophoretically homogeneous protein by heat treatment, salting-out, ion-exchange chromatography on DEAE-Sepharose CL-6 B, gel filtration on Sephadex G-50, and chromatofocusing on PBE 94. The inhibitor (FMCPI) was a single polypeptide with a molecular weight of 12000 and an isoelectric point of 5.2. It possessed the amino acid composition characterized by fairly high contents of aspartic acid, glutamic acid, and alanine and by no half-cystine. FMCPI was relatively thermostable since it maintained more than 50% of the original activity after treatment of 100°C for 20min at pH 2 or 7. However, the inhibitor almost lost its whole activity by the above treatment at pH 10. FMCPI inhibited papain in a 1:1 protein molar ratio: the Ki value was 2.4×10-11M. Complex formation between FMCPI and papain derivatives demonstrated that the inhibitor was capable of combining with even a papain molecule without the catalytic ability.
Journal
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- Nippon Shokuhin Kagaku Kogaku Kaishi
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Nippon Shokuhin Kagaku Kogaku Kaishi 47 (2), 105-111, 2000
Japanese Society for Food Science and Technology
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Keywords
Details 詳細情報について
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- CRID
- 1390282681387008000
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- NII Article ID
- 10007505303
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- NII Book ID
- AN10467499
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- ISSN
- 18816681
- 1341027X
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- NDL BIB ID
- 5277515
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- Text Lang
- ja
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- Data Source
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- JaLC
- NDL
- Crossref
- CiNii Articles
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- Abstract License Flag
- Disallowed