Messenger RNAs from the Scutellum and Aleurone of Germinating Barley Encode (1→3,1→4)-β-d-Glucanase, α-Amylase and Carboxypeptidase

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Abstract
Polyclonal antibodies raised against barley (1 .fwdarw. 3, 1 .fwdarw. 4)-.beta.-D-glucanase, .alpha.-amylase and carboxypeptidase were used to detect precursor polypeptides of these hydrolytic enzymes among the in vitro translation products of mRNA isolated from the scutellum and aleurone of germinating barley. In the scutellum, mRNA encoding carboxypeptidase appeared to be relatively more abundant than that encoding .alpha.-amylase or (1 .fwdarw. 3, 1 .fwdarw. 4)-.beta.-D-glucanase, while the aleurone .alpha.-amylase and (1 .fwdarw. 3, 1 .fwdarw. 4)-.beta.-D-glucansae mRNAs predominated. The apparent molecular weights of the precursors for (1 .fwdarw. 3, 1 .fwdarw. 4)-.beta.-D-glucanase, .alpha.-amylase, and carboxypeptidase were 33,000, 44,000, and 35,000, respectively. In each case these are slightly higher (1,500-5,000) than molecular weights of the mature enzymes. Molecular weights of precursors immunoprecipitated from aleurone and scutellum mRNA translation products were identical for each enzyme.