Phenylalanine ammonia-lyase of bamboo shoots.

• CHEN Ru-Yin

  Food Industry Research and Development Institute

• CHANG Tsung-Chain

  Food Industry Research and Development Institute

• LIU Ming-Sai

  Food Industry Research and Development Institute

Abstract

Phenylalanine ammonia-lyase (PAL) was purified from bamboo shoots (Bambusa oldhami Munro) through steps of DEAE-Sephacel column chromatography, Sepharose CL-6B gel filtration, and a second DEAE-Sephacel column chromatography. Polyacrylamide gel electrophoresis showed that the purified enzyme (M_r 360, 000) still contained two minor bands with much slower mobilities (M_r ?? 660, 000) than the major one. The minor band could be the aggregated forms of native PAL, based on the fact that only a single band (M_r 86, 000) was observed upon sodium dodecyl sulfate-polyacrylamide gel electrophoresis or isoelectric focusing, and all bands shared common antigenic determinants as revealed by immunoblotting done with an antiserum raised against the major band. There was a sharp rise of PAL activity of bamboo shoots after harvest, and this was only partly due to the de novo synthesis of this enzyme as measured by Laurell's rocket immunoelectrophoresis.

Journal

• Agricultural and Biological Chemistry

  Agricultural and Biological Chemistry 52 (9), 2137-2142, 1988

  Japan Society for Bioscience, Biotechnology, and Agrochemistry

Keywords

• General Agricultural and Biological Sciences
• General Biochemistry, Genetics and Molecular Biology

Details

• CRID: 1390282681441033216
• NII Article ID: 110006323972
• NII Book ID: AA00515312
• DOI: 10.1271/bbb1961.52.2137
• ISSN: 18811280
• ISSN: 00021369
• Text Lang: en
• Data Source:
  • JaLC
  • Crossref
  • CiNii Articles
• Abstract License Flag: Disallowed