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Alpha‐amylase inhibitor in cereals: Comparison of the protein in different rye, wheat and triticale seeds by using immunoblotting
Author(s) -
Sadowski Jan,
Macgregor Alexander,
Daussant Jean
Publication year - 1986
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/elps.1150070406
Subject(s) - triticale , isoelectric focusing , biology , amylase , antiserum , common wheat , isoelectric point , gene , biochemistry , enzyme , botany , genetics , antibody , chromosome
Several isoforms of the barley α‐amylase inhibitor were detected in the purified protein fraction and seed extract after isoelectric focusing. Polymorphism not detected by protein staining was revealed by immunoblotting using an antiserum against barley α‐amylase inhibitor. The antiserum, previously described as giving cross reactions with the inhibitors of rye and wheat, was used for comparing the electrophoretic patterns of the protein in several lines of rye, in several varieties of wheat and in different triticales. The antiserum was used for immunoblotting after isoelectric focusing at pH 3.5–10. The inhibitor was found in all samples but the degree of polymorphism was low. The same pattern was found for all lines of rye investigated. This pattern differed from the pattern found for wheat, but again, all cultivars of wheat investigated displayed similar patterns. Structural genes for the α‐amylase inhibitors were identified in the A and R genomes. Identical genes may exist on the B and D genomes. The wheat and rye structural genes for α‐amylase inhibitor were found to be expressed in the octoploid, hexaploid and tetraploid triticales.