TY - JOUR

T1 - Nucleotide sequence of a cDNA coding for the barley seed protein CMa

T2 - an inhibitor of insect α-amylase

AU - Rasmussen, Søren K.

AU - Johansson, Anette

PY - 1992/1/1

Y1 - 1992/1/1

N2 - The primary structure of the insect α-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 peptide of 25 amino acids. Ala and Leu account for 55% of the signal peptide. CMa is 60-85% identical with α-amylase inhibitors of wheat, but shows less than 50% identity to trypsin inhibitors of barley and wheat. The 10 Cys residues are located in identical positions compared to the cereal inhibitor family with a Pro-X-Cys motif present in all.

AB - The primary structure of the insect α-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 peptide of 25 amino acids. Ala and Leu account for 55% of the signal peptide. CMa is 60-85% identical with α-amylase inhibitors of wheat, but shows less than 50% identity to trypsin inhibitors of barley and wheat. The 10 Cys residues are located in identical positions compared to the cereal inhibitor family with a Pro-X-Cys motif present in all.

KW - CM protein

KW - Hordeum vulgare L.

KW - wheat

UR - http://www.scopus.com/inward/record.url?scp=0026455463&partnerID=8YFLogxK

U2 - 10.1007/BF00034972

DO - 10.1007/BF00034972

M3 - Journal article

C2 - 1732002

AN - SCOPUS:0026455463

VL - 18

SP - 423

EP - 427

JO - Plant Molecular Biology

JF - Plant Molecular Biology

SN - 0167-4412

IS - 2

ER -