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γ‐Purothionins: amino acid sequence of two polypeptides of a new family of thionins from wheat endosperm

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Colilla, Francisco J., Rocher, Asuncion, Mendez, Enrique·1990·FEBS Letters

Abstract

Two homologous sulfur‐rich basic polypeptides form wheat endosperm, so‐called γ 1‐purothionin and γ 2‐purothionin, are described. Purification involves extraction with volatile solvents and ammonium bicarbonate fractionation followed by reversed‐phase high‐performance liquid chromatography. The complete primary structure of these two polypeptides has been determined by automatic degradation of the intact, S‐carboxymethylated γ‐purothionins and peptides obtained by enzymatic cleavage. γ 1‐Purothionin and γ 2‐purothionin consist of 47 amino acids with an assessed molecular weight of 5239 and 5151 Da, respectively and 8 cysteines organized in 4 disulfide bridges. They present a high degree of homology among themselves (89% of identity) and are the first two thionin‐like polypeptides, so‐called y‐thionins, described from wheat endosperm.

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Metadata

Authors
Colilla, F. J., Rocher, A., & Mendez, E.
Venue
FEBS Letters
Publisher
Wiley
Published
1990-09-17
Volume
270
Issue
1-2
Pages
191-194
ISSN
  • 0014-5793 (ISSN-L)
  • 1873-3468
OpenAlex
W2083637991
Cited by
223
References
0
FWCI
2.39
Type
journal article
Language
en
Open access
bronze

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CoChat. (2026). Citation check: γ‐Purothionins: amino acid sequence of two polypeptides of a new family of thionins from wheat endosperm. https://app.cochat.ai/papers/10.1016/0014-5793(90)81265-p
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Colilla, F. J., Rocher, A., & Mendez, E. (1990). γ‐Purothionins: amino acid sequence of two polypeptides of a new family of thionins from wheat endosperm. FEBS Letters. https://doi.org/10.1016/0014-5793(90)81265-p

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