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Polymorphisms in the α-Amy1 Gene of Wild and Cultivated Barley Revealed by the Polymerase Chain Reaction by S. Weining; L. Ko; R. J. Henry is a Agricultural and Biological Sciences article available to read on EtoBox.

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α-Amylases are the key enzymes involved in the hydrolysis of starch in plants. The polymerase chain reaction (PCR) was used to detect polymorphisms in the length of amplified sequences between the annealing sites of two primers derived from published α-amy1 gene sequences in barley. These two primers (Bsw1 and Bsw7), flanking the promoter region and the first exon, amplified two PCR fragments in barley. One of the amplified products, with the expected length of 820 bp, appeared together with another shorter PCR band of around 750 bp. This 750-bp fragment seems to be derived from an α-amylase gene not reported previously. Both of the PCR products could be amplified from the two-rowed barley varieties tested, including cv Himalaya from which the sequence information was obtained. Five of the six-rowed barley varieties also have the two PCR fragments whereas another two have only the long fragment. These two fragments seem to be unique to barley, neither of them could be amplified from other cereals; for example, wheat, rye or sorghum. These two α-amylase fragments were mapped to the long arm of 6H, the location of the α-amy1 genes, using wheat-barley addition lines. Amplification of

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Author

S. Weining; L. Ko; R. J. Henry

Publisher

Springer; Springer-Verlag; Springer Verlag; Springer Science and Business Media LLC; Society for Mining, Metallurgy and Exploration Inc.; Springer Nature (ISSN 0040-5752)

Published

1994

Language

EN

Field

Agricultural and Biological Sciences (Life Sciences)