𝔖 Bobbio Scriptorium
✦   LIBER   ✦

A dimeric inhibitor or insect α-amylase from barley : Cloning of the cDNA and identification of the protein

✍ Scribed by Ana LÁZARO; Rosa SANCHEZ-MONGE; Gabriel SALCEDO; Javier PAZ-ARES; Pilar CARBONERO; Francisco GARCÍA-OLMEDO

Book ID
115125618
Publisher
John Wiley and Sons
Year
1988
Tongue
English
Weight
593 KB
Volume
172
Category
Article
ISSN
1432-1327

No coin nor oath required. For personal study only.

📜 SIMILAR VOLUMES

Nucleotide sequence of a cDNA coding for
Nucleotide sequence of a cDNA coding for the barley seed protein CMa: an inhibitor of insect α-amylase
✍ Søren K. Rasmussen; Anette Johansson 📂 Article 📅 1992 🏛 Springer 🌐 English ⚖ 361 KB

The primary structure of the insect alpha-amylase inhibitor CMa of barley seeds was deduced from a full-length cDNA clone pc43F6. Analysis of RNA from barley endosperm shows high levels 15 and 20 days after flowering. The cDNA predicts an amino acid sequence of 119 residues preceded by a signal pept

Cloning of cDNA, expression, and chromos
Cloning of cDNA, expression, and chromosomal location of genes encoding the three types of subunits of the barley tetrameric inhibitor of insect α-amylase
✍ Joaquin Medina; Gregorio Hueros; Pilar Carbonero 📂 Article 📅 1993 🏛 Springer 🌐 English ⚖ 834 KB

Three cDNA clones from barley developing endosperm, corresponding to proteins BTAI-CMa, BTAI-CMb and BTAI-CMd, which are the three types of subunits of the tetrameric inhibitor of insect c~-amylases, have been identified and sequenced. The deduced amino acid sequence of BTAI-CMb corresponds to the C

A major barley allergen associated with
A major barley allergen associated with baker's asthma disease is a glycosylated monomeric inhibitor of insect α-amylase: cDNA cloning and chromosomal location of the gene
✍ Montaña Mena; Rosa Sanchez-Monge; Luis Gomez; Gabriel Salcedo; Pilar Carbonero 📂 Article 📅 1992 🏛 Springer 🌐 English ⚖ 881 KB

A 14.5 kDa barley endosperm protein that is a major allergen in baker's asthma disease, as previously shown by both in vitro (IgE binding) and in vivo tests, has been identified as a glycosylated monomeric member of the multigene family of inhibitors of e-amylase/trypsin from cereals. A cDNA encodin