7 rezultatus
We have isolated and characterized cDNA clones encoding avenins, the prolamine storage proteins of oat seeds. Sequence analysis shows that avenins are a related group of polypeptides and that their mRNAs differ from each other by point mutations and small insertions and deletions. Avenin proteins
A procedure for the isolation and sequence analysis of the "fast" avenin component (N9) from the oat (Avena sativa L., cv. Narymsky 943) is described. Component N9 was prepared by an ion-exchange high-performance liquid chromatography on a strong cation exchange column type Mono S (Pharmacia,
We have elucidated the complete amino acid sequence of one of the avenin components, avenin-3, isolated from oat (Avena sativa L.), variety Narymsky 943. The sequence of the protein was determined by sequencing of CNBr and trypsin-generated peptides in combination with mass spectrometry. The protein
The seed storage proteins of oats (Avena sativa L.) are synthesized and assembled into vacuolar protein bodies in developing endosperm tissue. We used double-label immunolocalization to study the distribution of these proteins within protein bodies of the starchy endosperm. When sections of
BACKGROUND
The oat seed storage proteins are mainly composed of two classes: the globulins and avenins. Among the major cereals, the globulins are the major seed protein class in rice and oats, and along with the higher protein content of oats is the basis for the relative higher nutrition content
Six chloroform/methanol-soluble proteins from oat endosperm (Avena sativa) have been isolated and characterized by a purification procedure based on extraction with volatile solvents, followed by reversed-phase high performance liquid chromatography. Three of these proteins, with an assessed
During the 20th century, the economic position of oats (Avena sativa L.) decreased strongly in favour of higher yielding crops including winter wheat and maize. Presently, oat represents only ~1.3% of the total world grain production, and its production system is fragmented. Nonetheless, current