Purification and Some Properties of Three Chitinases from the Seeds of Rye (Secale cereale)

Takeshi Yamagami, Gunki Funatsu

研究成果: ジャーナルへの寄稿記事

37 引用 (Scopus)

抄録

Three chitinases, designated RSC-a, -b, and -c, were purified from the seeds of rye (Secale cereal) using ammonium sulfate precipitation, CM-cellulose column chromatography, gel filtration on Sephadex G-75, and S-Sepharose column chromatography. RSC-a, -b, and -c are basic proteins having molecular masses of 33 kDa, 26 kDa, and 26 kDa, and isoelectric points of 9.7, 10, and >10, respectively. RSC-b and -c were found to be homologous proteins having similar amino acid compositions and N-terminal sequences. RSC-a contains more Thr, Ser, Glu, Pro, Gly, and Cys than RSC-b and -c and has a different N-terminal sequence from them. They hydrolyze glycolchitin and colloidal chitin, but not cell walls of Micrococcus lysodeikticus. These enzymes are stable at pH 4-8 and their optimum pHs toward glycolchitin are 5.

元の言語英語
ページ(範囲)643-647
ページ数5
ジャーナルBioscience, Biotechnology and Biochemistry
57
発行部数4
DOI
出版物ステータス出版済み - 1 1 1993

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Chitinases
Column chromatography
Purification
Seed
Seeds
Micrococcus
Agarose Chromatography
Chitin
Isoelectric Point
Ammonium Sulfate
Molecular mass
Cellulose
Sepharose
Cell Wall
Gel Chromatography
Proteins
Gels
Cells
Amino Acids
Enzymes

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Analytical Chemistry
  • Biochemistry
  • Applied Microbiology and Biotechnology
  • Molecular Biology
  • Organic Chemistry

これを引用

Purification and Some Properties of Three Chitinases from the Seeds of Rye (Secale cereale). / Yamagami, Takeshi; Funatsu, Gunki.

:: Bioscience, Biotechnology and Biochemistry, 巻 57, 番号 4, 01.01.1993, p. 643-647.

研究成果: ジャーナルへの寄稿記事

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