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Related Experiment Videos

Characterization of a maize root proteinase

V J Goodfellow1, L P Solomonson, A Oaks

  • 1Botany Department, University of Guelph, Ontario, Canada.

Plant Physiology
|February 1, 1993
PubMed
Summary

This study identifies a specific maize root proteinase that cleaves peptide bonds after alanine residues. This serine endopeptidase

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Area of Science:

  • Plant Biochemistry
  • Enzymology
  • Proteomics

Background:

  • Maize (Zea mays) root proteinase is a serine endopeptidase.
  • This enzyme may regulate nitrate assimilation by turning over nitrate reductase (NR).

Purpose of the Study:

  • To determine the specificity and uniqueness of the maize root proteinase.
  • To investigate its potential role in nitrate assimilation.

Main Methods:

  • Used bovine serum albumin and purified Chlorella vulgaris NR as substrates.
  • Analyzed proteolytic fragments using microsequence analysis and carboxypeptidase Y.
  • Generated peptide maps for comparison with other serine endopeptidases.

Main Results:

  • Maize root proteinase preferentially cleaves at alanine residues on the amino side of the scissile bond.
  • Specific cleavage sites identified in Chlorella NR and bovine serum albumin.
  • Peptide map of maize root proteinase is unique compared to elastase, trypsin, and chymotrypsin.

Conclusions:

  • Maize root proteinase cleaves peptide bonds at the carboxy side of alanine.
  • The enzyme's specificity suggests potential applications in protein chemistry.
  • Further research could clarify its physiological role in nitrate assimilation.

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