Purification and differential expression of enolase from maize

Shailesh K. Lal, Philip M. Kelley, Thomas F. Elthon

Research output: Contribution to journalArticlepeer-review

12 Scopus citations


Enolase was purified from maze (Zea mays L. inbred B73)seeds to a 55 and 56 kDa protein doublet based upon sodium dodecyl sulfate – polyacrylamide gel electrophoresis. Purification included ammonium sulfate‐precipitation, gel filtration, Mono Q, and Phenyl Superose chromatography. Two‐dimensional gels further resolved the 56 kDa protein into three isoselectric forms. Polyclonal antibodies raised against the purified proteins, were found to bind specifically to both the 55 and 56 kDa proteins during purification. Theses antibodies did not recognized a 56 kDa protein when the strain was complemented with maize enolase (pZM245). Maize enolase antibodies recognized a extracts indicated that the 55 kDa form of enolase was more abundant in roots. Enolase protein levels remained unchanged in maize roots after 24 h of anaerobiosis, even though the specific activity of enolase increased to twice its initial levels. A plastid form of enolase in maize could not be found as either enolase activity or protein (with immunoblots).

Original languageEnglish (US)
Pages (from-to)587-592
Number of pages6
JournalPhysiologia Plantarum
Issue number4
StatePublished - Aug 1994
Externally publishedYes


  • Anaerobic stress
  • Zea mays
  • antibodies
  • enolase
  • glycolysis
  • maize
  • purification
  • purification
  • tissue specific expression
  • tissue specific expression

ASJC Scopus subject areas

  • Physiology
  • Genetics
  • Plant Science
  • Cell Biology


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