Isolation of a complementary DNA encoding the bean PR4 chitinase: an acidic enzyme with an amino-terminus cysteine-rich domain View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1991-08

AUTHORS

Marcia Margis-Pinheiro, Marie Hélène Metz-Boutigue, Abalo Awade, Marc de Tapia, Monique le Ret, Géraud Burkard

ABSTRACT

The amino acid sequences of peptides generated by trypsin and chymotrypsin digestions of the acidic PR4 chitinase from bean were determined. Oligonucleotide primers derived from this sequence were used to synthesize a PR4 chitinase-specific probe by PCR-amplification. This probe allowed the isolation of cDNA clones encoding PR4 chitinase that have been sequenced. This acidic and extracellular chitinase shows some homology to the basic isoform from the same plant, and differs from other known acidic chitinases by the presence of an amino-terminal cysteine-rich domain. Southern blot analysis of bean genomic DNA revealed that PR4 chitinase is encoded by a single gene. More... »

PAGES

243-253

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/bf00039499

DOI

http://dx.doi.org/10.1007/bf00039499

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1051898369

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/1863776


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