• Corpus ID: 208555025

A multigene family from cereals which encodes inhibitors of trypsin and heterologous a-amylases

  title={A multigene family from cereals which encodes inhibitors of trypsin and heterologous a-amylases},
  author={Pilar Carbonero Zalduegui and Gabriel Salcedo Duran and Rosa S{\'a}nchez-Monge Laguna de Rins and Federico Garc{\'i}a Maroto and Joaqu{\'i}n Royo and Luis G{\'o}mez and Monta{\~n}a Mena and Joaqu{\'i}n Medina Alcazar and Isabel Diaz Rodriguez},
Plant proteins that are inhibitory towards various types of hydrolases from heterologous systems (fungi, insects, vertebrates, etc.) have been extensively studied. The crystallization of a trypsin inhibitor from soybean and of its complex with trypsin, which was carried out by Kunitz over forty years ago, was one major achievement in the early stages of research on protein inhibitors from plants. Recent advances in molecular biology of these inhibitors have greatly increased our… 
A multigene family of trypsin/a-amylase inhibitors from cereals
In wheat and barley, a substantial fraction of the total endosperm protein content is represented by toxins and inhibitors that are active towards heterologous systems, and some of them can be selectively extracted with chloroform/methanol mixtures and have therefore been designated CM-proteins.
A Multigene Family of Trypsin/α-Amylase Inhibitors from Cereals
Advances in the molecular biology of proteinaceous inhibitors of hydrolases have greatly increased knowledge of their structure and in vitro properties, and have allowed previously unsuspected relationships between functionally different proteins to be established.
Cereal α-amylase/trypsin inhibitors and transgenic insect resistance
Preliminary data with other transgenically expressed members of the family confirmed the potential of these inhibitors for increasing insect resistance in genetically modified plants (GMP), and aimed at complementing an integrated pest management system, by amplifying the natural variability outside the species barrier.
Rye chromosome arm 3RS encodes a homodimeric inhibitor of insect α-amylase
A new inhibitor of insect α-amylase, designated RDAI-1, has been purified from rye (Secale cereale L.) endosperm. RDAI-1 is homologous to wheat homodimeric inhibitors. This homology is supported by
Wheat and Barley Inhibitors Active Towards α-Amylase and Trypsin-like Activities from Spodoptera frugiperda
The α-amylase activity was determined throughout the larval development of Spodoptera frugiperda and none of the other larval digestive protease activities were inhibited, indicating that the barley inhibitor is specific towards trypsin-like enzymes.
Comparative phylogenetic analysis of cystatin gene families from arabidopsis, rice and barley
This cystatin classification should facilitate the assignment of proteinase specificities and functions to other cystatins as new information is obtained.
Sharp divergence between wheat and barley at loci encoding novel members of the trypsin/α-amylase inhibitors family
Southern analysis of DNAs from diploids, tetraploid, and hexaploid wheats, as well as from aneuploid lines, indicate that there is a single CMx locus in each of the three genomes of hexaPloid wheat, respectively associated with chromosomal arms 4AS, 4BS, and 4DL.
Seed Proteins
Electrophoretic patterns of seed albumins in the old-world lupinus species: variation in the 2S albumin class.
Inhibitory activities against heterologous α-amylases and in vitro allergenic reactivity of Einkorn wheats
Salt extracts from seeds of 36 lines of Einkorn wheats were analyzed for their inhibitory activity towards two insect (Tenebrio molitor, Coleoptera, and Ephestia kuehniella, Lepidoptera) and one
Characterization of a barley gene coding for an α-amylase inhibitor subunit (CMd protein) and analysis of its promoter in transgenic tobacco plants and in maize kernels by microprojectile bombardment
Promoters of the Hv85.1 CMd protein gene promoter, when fused to a gus coding region, were unable to direct GUS activity in the seeds of transgenic tobacco plants, but the same construction delivered into immature maize kernels by microprojectile bombardment was able to direct expression of GUS in the outermost cell layers of maize endosperm in both a tissue-specific and a developmentally determined manner.