2002年2月
Isolation and characterization of a cysteine protease of freesia corms
BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY
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- 巻
- 66
- 号
- 2
- 開始ページ
- 448
- 終了ページ
- 452
- 記述言語
- 英語
- 掲載種別
- DOI
- 10.1271/bbb.66.448
- 出版者・発行元
- TAYLOR & FRANCIS LTD
A protease, freesia protease (FP)-A, was purified to electrophoretic homogeneity from regular freesia (Freesia reflacta) corms in harvest time. The M, of FP-A was estimated to be 24 k by SDS-PAGE. The optimum pH of the enzyme was 8.0 using a casein substrate. These enzymes were strongly inhibited by p-chloromercuribenzoic acid but not by phenylmethane-sulfonylfluoride and EDTA. These results indicate that FP-A belongs to the cysteine proteases. The amino terminal sequence of FP-A was similar to that of papain, and the sequences was regarded to the conservative residues of cysteine protease. From the hydrolysis of peptidyl-p-NAs, the specificity of FP-A was found to be broad. It was thought that FP-A was a new protease from freesia corms.
- リンク情報
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- DOI
- https://doi.org/10.1271/bbb.66.448
- CiNii Articles
- http://ci.nii.ac.jp/naid/110002693671
- PubMed
- https://www.ncbi.nlm.nih.gov/pubmed/11999426
- Web of Science
- https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000174150400035&DestApp=WOS_CPL
- ID情報
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- DOI : 10.1271/bbb.66.448
- ISSN : 0916-8451
- eISSN : 1347-6947
- CiNii Articles ID : 110002693671
- PubMed ID : 11999426
- Web of Science ID : WOS:000174150400035