Plants and the study of serpin biology

Thomas H. Roberts, Joon Woo Ahn, Nardy Lampl, Robert Fluhr

Research output: Chapter in Book/Report/Conference proceedingChapterpeer-review

7 Scopus citations

Abstract

Serpins appear to be ubiquitous in the Plant Kingdom and have several unique properties when compared to the substantial number of other families of protease inhibitors in plants. Serpins in plants are likely to have functions distinct from those of animal serpins, partly because plants and animals developed multicellularity independently and partly because most animal serpins are involved in animal-specific processes, such as blood coagulation and the activation of complement. To encourage and facilitate the discovery of plant serpin functions, here we provide a set of protocols for detection of serpins in plant extracts, localization of serpins in plant tissues and cells, purification of serpins from a range of organs from monocot and eudicot plants, production and purification of recombinant plant serpins, and analysis of plantprotease interactions including identification of in vivo target proteases.

Original languageAmerican English
Title of host publicationMethods in Enzymology
PublisherAcademic Press Inc.
Pages347-366
Number of pages20
DOIs
StatePublished - 2011
Externally publishedYes

Publication series

NameMethods in Enzymology
Volume499
ISSN (Print)0076-6879
ISSN (Electronic)1557-7988

Keywords

  • Arabidopsis
  • AtSerpin1
  • Biotinylated protease
  • Cereal grain
  • Complex formation
  • Cysteine protease
  • DCG-04
  • E-64
  • Immunoprecipitation
  • Mechanism-based probe
  • Native-PAGE
  • Non-reducing gel
  • Plant
  • Protease inhibitor
  • Protein purification
  • Protoplast
  • RD-21
  • Recombinant protein
  • SDS-PAGE
  • Serine protease
  • Serpin
  • Subcellular localization
  • T-DNA mutant
  • Thiol extraction
  • Thiophillic adsorption chromatography

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