THERMAL ACTIVATION OF PEROXIDASE FROM TOBACCO LEAF MESOPHYLL CELL WALLS

YUEN‐MIN ‐M CHOY, YUM‐SHING ‐S WONG, KIT‐MAN ‐M LAU, KUNG HYUNG*

*Corresponding author for this work

Research output: Contribution to journalJournal Articlepeer-review

Abstract

Cell wall‐bound peroxidase isolated from tobacco leaf mesophll cell walls was found to consist of two isoenzymes (P1 and P2). Each exists in the form of a single subunit with the same molecular weight (35 000) as determined by Sodium dodecyl sulphate (SDS) polyacrylamide gel electrophoresis. Both isoenzymes exhibited maximum activities at 70°. P1 increased to 265% and P2 to 140% of the activities assayed at 27°; below this temperature the two isoenzymes had the same specific activity. On hydrolysis, P1 showed a carbohydrate content of 26.22% when the monosaccharides were analyzed by gas liquid chromatography; P2 gave 21.45%.

Original languageEnglish
Pages (from-to)1-4
Number of pages4
JournalInternational Journal of Peptide and Protein Research
Volume14
Issue number1
Publication statusPublished - Jul 1979
Externally publishedYes

Keywords

  • carbohydrate contents of isoperoxidases
  • isoperoxidases
  • peroxidases
  • thermal activation
  • tobacco leaf isoperoxidases

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