BIOMAT Database Logo BIOMAT Database Logo

Amino acid sequence of a purothionin homolog from barley flour. 1980

Y Ozaki, and K Wada, and T Hase, and H Matsubara, and T Nakanishi, and H Yoshizumi

A purothionin homolog was isolated from barley flour and purified by CM-52 column chromatography. It showed potent lethal activity towards brewer's yeast and its complete amino acid sequence was determined to be as follows. Lys-Ser-Cys-Cys-Arg-Ser-Thr-Leu-Gly-Arg-Asn-Cys-Tyr-Asn-Leu-Cys-Arg-Val-Arg-Gly-Ala-Gln-Lys-Leu-Cys-Ala-Gly-Val-Cys-Arg-Cys-Lys-Leu-Thr-Ser-Ser-Gly-Lys-Cys-Pro-Thr-Gly-Phe-Pro-Lys. It thus consists of 45 amino acid residues with 8 cysteines. The number of amino acid residues and the positions of the 8 cysteines are identical with those of wheat purothionins. There is a high degree of homology in the primary structures of these proteins.

UI MeSH Term Description Entries
D010940 Plant Proteins Proteins found in plants (flowers, herbs, shrubs, trees, etc.). The concept does not include proteins found in vegetables for which PLANT PROTEINS, DIETARY is available. Plant Protein,Protein, Plant,Proteins, Plant
D002845 Chromatography Techniques used to separate mixtures of substances based on differences in the relative affinities of the substances for mobile and stationary phases. A mobile phase (fluid or gas) passes through a column containing a stationary phase of porous solid or liquid coated on a solid support. Usage is both analytical for small amounts and preparative for bulk amounts. Chromatographies
D005075 Biological Evolution The process of cumulative change over successive generations through which organisms acquire their distinguishing morphological and physiological characteristics. Evolution, Biological
D000595 Amino Acid Sequence The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D001467 Hordeum A plant genus of the family POACEAE. The EDIBLE GRAIN, barley, is widely used as food. Barley,Hordeum vulgare
D012441 Saccharomyces cerevisiae A species of the genus SACCHAROMYCES, family Saccharomycetaceae, order Saccharomycetales, known as "baker's" or "brewer's" yeast. The dried form is used as a dietary supplement. Baker's Yeast,Brewer's Yeast,Candida robusta,S. cerevisiae,Saccharomyces capensis,Saccharomyces italicus,Saccharomyces oviformis,Saccharomyces uvarum var. melibiosus,Yeast, Baker's,Yeast, Brewer's,Baker Yeast,S cerevisiae,Baker's Yeasts,Yeast, Baker
D023181 Antimicrobial Cationic Peptides Small cationic peptides that are an important component, in most species, of early innate and induced defenses against invading microbes. In animals they are found on mucosal surfaces, within phagocytic granules, and on the surface of the body. They are also found in insects and plants. Among others, this group includes the DEFENSINS, protegrins, tachyplesins, and thionins. They displace DIVALENT CATIONS from phosphate groups of MEMBRANE LIPIDS leading to disruption of the membrane. Cationic Antimicrobial Peptide,Cationic Antimicrobial Peptides,Cationic Host Defense Peptides,Host Defense Peptide,Microbicidal Cationic Proteins,Amphipathic Cationic Antimicrobial Peptides,Host Defense Peptides,Antimicrobial Peptide, Cationic,Antimicrobial Peptides, Cationic,Cationic Peptides, Antimicrobial,Cationic Proteins, Microbicidal,Defense Peptide, Host,Defense Peptides, Host,Peptide, Cationic Antimicrobial,Peptide, Host Defense,Peptides, Antimicrobial Cationic,Peptides, Cationic Antimicrobial,Peptides, Host Defense,Proteins, Microbicidal Cationic

Related Publications

Y Ozaki, and K Wada, and T Hase, and H Matsubara, and T Nakanishi, and H Yoshizumi
The amino acid sequence of wheat beta-purothionin.
October 1976, Canadian journal of biochemistry,
Y Ozaki, and K Wada, and T Hase, and H Matsubara, and T Nakanishi, and H Yoshizumi
The amino-acid sequence of a purothionin from Triticum monococcum, a diploid wheat.
July 1983, European journal of biochemistry,
Y Ozaki, and K Wada, and T Hase, and H Matsubara, and T Nakanishi, and H Yoshizumi
The complete amino acid sequence of barley trypsin inhibitor.
July 1983, The Journal of biological chemistry,
Y Ozaki, and K Wada, and T Hase, and H Matsubara, and T Nakanishi, and H Yoshizumi
Detection, isolation and complete amino acid sequence of an aeroallergenic protein from rapeseed flour.
July 1997, Clinical and experimental allergy : journal of the British Society for Allergy and Clinical Immunology,
Y Ozaki, and K Wada, and T Hase, and H Matsubara, and T Nakanishi, and H Yoshizumi
Wheat albumin and globulin proteins: purothionin levels of stored flour.
July 1976, Journal of the science of food and agriculture,
Y Ozaki, and K Wada, and T Hase, and H Matsubara, and T Nakanishi, and H Yoshizumi
Amino acid sequence of bovine protein Z: a vitamin K-dependent serine protease homolog.
May 1985, FEBS letters,
Y Ozaki, and K Wada, and T Hase, and H Matsubara, and T Nakanishi, and H Yoshizumi
Amino acid sequence in the proteolytic glycopeptide of barley stripe mosaic virus.
May 1977, Virology,
Y Ozaki, and K Wada, and T Hase, and H Matsubara, and T Nakanishi, and H Yoshizumi
Nucleotide sequence of a cDNA from Atriplex canescens (Pursh.) Nutt. A homolog of a jasmonate-induced protein from barley.
July 1995, Plant physiology,
Y Ozaki, and K Wada, and T Hase, and H Matsubara, and T Nakanishi, and H Yoshizumi
Complete primary structures of two subunits of purothionin A, a lethal protein for brewer's yeast from wheat flour.
September 1977, Journal of biochemistry,
Y Ozaki, and K Wada, and T Hase, and H Matsubara, and T Nakanishi, and H Yoshizumi
cDNA, amino acid and carbohydrate sequence of barley seed-specific peroxidase BP 1.
April 1992, Plant molecular biology,
Copied contents to your clipboard!