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CHARACTERIZATION OF PARTIALLY PURIFIED GLUTATHIONE REDUCTASE FROM COLD-HARDENED AND NONHARDENED SPINACH LEAF TISSUE.

Author(s) : GUY C. L., CARTER J. V.

Type of article: Article

Summary

GLUTATHIONE REDUCTASE (GR) WAS STUDIED IN CRUDE AND PARTIALLY PURIFIED EXTRACTS FROM NONHARDENED 298/293 K D/N (25/20 DEG C) AND HARDENED 278 K/278 K D/N (5/5 DEG C) SPINACH-LEAF TISSUE. THE PARTIALLY PURIFIED ENZYME FROM THE TWO SOURCES SHOWED DIFFERENT KINETIC CHARACTERISTICS, HEAT INACTIVATION, FREEZING INACTIVATION, AND ELECTROPHORETIC MOBILITIES. HARDENED LEAVES CONTAIN DIFFERENT FORMS OF GLUTATHIONE REDUCTASE THAN DO NONHARDENED LEAVES. GR FROM HARDENED SPINACH HAS GREATER STABILITY AGAINST FREEZING AND A HIGHER AFFINITY FOR SUBSTRATES AT LOW TEMPERATURE THAN DOES GR FROM NONHARDENED SPINACH.

Details

  • Original title: CHARACTERIZATION OF PARTIALLY PURIFIED GLUTATHIONE REDUCTASE FROM COLD-HARDENED AND NONHARDENED SPINACH LEAF TISSUE.
  • Record ID : 1985-1108
  • Languages: English
  • Source: Cryobiology - vol. 21 - n. 4
  • Publication date: 1984

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