P2065
Purothionin from whole wheat flour
Mixture of α- and β-isomers, lyophilized powder, 0.25-1.0 units/mg protein
biological source
whole wheat flour
form
lyophilized powder
specific activity
0.25-1.0 units/mg protein
composition
Protein, ~90%
UniProt accession no.
storage temp.
−20°C
Gene Information
wheat ... Pur-B1(543304)
Biochem/physiol Actions
In conjunction with thioredoxin, affects proper protein folding; cytotoxic, presumably by forming pores in cytoplasmic membrane.
Other Notes
One unit will cause a ΔA650 of 1.0 per min (increase the turbidity) of a 1 mg/ml solution of bovine insulin in the presence of 2 mM EDTA and 0.33 mM DTT at pH 7.5 at 37 °C.
Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
Regulatory Information
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Purification and partial characterization of a 31-kDa cysteine endopeptidase from germinated barley.
N Zhang et al.
Planta, 199(4), 565-572 (1996-01-01)
Proteolytic enzymes hydrolyze cereal seed storage proteins into small peptides and amino acids, which are very important for seed germination and the malting process. A cysteine-class endopeptidase was purified from 4-d-germinated barley (Hordeum vulgare L. cv. Morex). Four purification steps
T C Johnson et al.
Plant physiology, 85(2), 446-451 (1987-10-01)
Thioredoxin h, the thioredoxin characteristic of heterotrophic plant tissues, was purified to homogeneity from wheat endosperm (flour) and found to resemble its counterpart from carrot cell cultures. In the presence of NADPH, homogeneous thioredoxin h and partially purified wheat endosperm
Okumura, K., et al.
Agricultural and Biological Chemistry, 53, 3303-3303 (1989)
G Nitti et al.
European journal of biochemistry, 228(2), 250-256 (1995-03-01)
The complete primary structure of a new alpha-amylase inhibitor from Sorghum bicolor belonging to the gamma-thionin family has been determined and the amino acid sequences of two components of the family already elucidated have been corrected by combining the classical
M Bruix et al.
Biochemistry, 32(2), 715-724 (1993-01-19)
The complete assignment of the proton NMR spectra of the homologous gamma 1-hordothionin and gamma 1-purothionin (47 amino acids, 4 disulfide bridges) from barley and wheat, respectively, has been performed by two-dimensional sequence-specific methods. A total of 299 proton-proton distance
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