Subunit structure of canavalin

Rimona Margalit*, Ezra Daniel

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

1 Scopus citations

Abstract

The subunit structure of canavalin was studied. The native protein has a sedimentation coefficient of 6.4 S and a MW of 91 000. SDS gel electrophoresis of the fully dissociated protein gave a single band, corresponding to a polypeptide chain with a MW of 22700. A minimal MW of 20700 was estimated from the amino acid composition. On a MW basis the native molecule consists of 4 chains. Support for the tetrameric structure of canavalin is provided by the electrophoretic pattern of partially dissociated protein.

Original languageEnglish
Pages (from-to)1015-1016
Number of pages2
JournalPhytochemistry
Volume17
Issue number6
DOIs
StatePublished - 1978

Keywords

  • Canavalia ensiformis
  • Leguminosae
  • canavalin
  • jack beans
  • proteins.
  • subunit structure

Fingerprint

Dive into the research topics of 'Subunit structure of canavalin'. Together they form a unique fingerprint.

Cite this