Association of a 33-kilodalton cysteine proteinase found in corn callus with the inhibition of fall armyworm larval growth

Binghua Jiang, Ulfah Siregar, Kenneth O. Willeford, Dawn S. Luthe, W. Paul Williams

Research output: Contribution to journalArticle

39 Scopus citations

Abstract

Protein patterns of callus from corn (Zea mays L.) inbreds that are either resistant or susceptible to fall armyworm (Spodoptera frugiperda [J.E. Smith]) were analyzed by two-dimensional electrophoresis. Fall armyworm larvae reared on callus initiated from resistant inbreds were significantly smaller than those reared on callus of susceptible inbreds. A 33-kD protein found in callus from the resistant inbreds Mp704 and Mp708 was absent in callus from the susceptible inbreds Tx601 and Ab24E. However, a 36-kD protein found in Ab24E callus immunoreacted with polyclonal antibody raised against the 33-kD protein. When Mp704 nonfriable callus changed to friable, larval growth was not inhibited and the 33-kD protein was absent. There was a significant negative correlation between the concentration of the 33-kD protein in the callus and the weight of the larvae feeding on the callus in the F2 progeny of Mp704 x Tx601. The N-terminal amino acid sequence of the 33-kD protein suggested that it was cysteine proteinase. Purification of the 33- (Mp708) and 36-kD (Ab24E) proteins indicated that they were both cysteine proteinases. The 33-kD cysteine proteinase had 7-fold higher specific activity than the 36-kD enzyme.

Original languageEnglish (US)
Pages (from-to)1631-1640
Number of pages10
JournalPlant physiology
Volume108
Issue number4
DOIs
StatePublished - Aug 1995

All Science Journal Classification (ASJC) codes

  • Physiology
  • Genetics
  • Plant Science

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