Purification, crystallization, and molecular properties of aspartase from Pseudomonas fluorescens.

• TAKAGI Jun S.

  Department of Chemistry, Faculty of Science, Kyoto University

• FUKUNAGA Rikiro

  Institute for Virus Research, Kyoto University

• TOKUSHIGE Masanobu

  Department of Chemistry, Faculty of Science, Kyoto University

• KATSUKI Hirohiko

  Department of Chemistry, Faculty of Science, Kyoto University

抄録

Aspartase [L-aspartate ammonia-lyase, EC 4. 3. 1. 1] of Pseudomonas fluorescens was highly purified to homogeneity and crystallized. The purified enzyme sedimented as a monodisperse entity upon ultracentrifugation with a s⁰_{20, w} value of 8.6 S. Upon polyacrylamide gel electrophoresis (PAGE), the enzyme migrated as a single band. The molecular weight of the native enzyme was 173, 000±3, 000, as determined by sedimentation equilibrium analysis, and that of the enzyme subunit was determined to be 50, 000±1, 500 by sodium dodecyl sulfate (SDS)-PAGE. Cross-linking experiments using dimethyl suberimidate followed by SDS-PAGE indicated that the native enzyme was composed of four subunits with identical molecular weight. The amino acid composition of the enzyme was determined.

収録刊行物

• The Journal of Biochemistry

  The Journal of Biochemistry 96 (2), 545-552, 1984

  The Japanese Biochemical Society

詳細情報

• CRID: 1573105977924525184
• NII論文ID: 130003542969
• ISSN: 0021924X
• Web Site: https://jlc.jst.go.jp/DN/JALC/00169693433?from=CiNii
• 本文言語コード: en
• データソース種別:
  • CiNii Articles