| Literature DB >> 6208985 |
J A Erratt, P E Douglas, F Moranelli, V L Seligy.
Abstract
The induction of alpha-amylase by starch has been studied in the filamentous fungus Aspergillus oryzae. Low levels of alpha-amylase activity were found in both intracellular and extracellular samples from glucose-grown cultures. However, alpha-amylase activity increased when starch was the sole carbon source. The intracellular enzyme activity was induced by a factor of approximately 6.5, while the extracellular activity increased 20-fold over that found in the glucose-grown cultures. Regardless of the carbon source or cellular location, the molecular weight of the active protein was 52 500 +/- 1800 and only this protein reacted with antibodies specific for alpha-amylase. A parallel study of the in vitro translated proteins directed by poly(A)+ RNA fractions indicated a presumptive alpha-amylase with a similar isoelectric point but with a molecular weight of approximately 54 000. This protein was most prevalent using RNA from early, exponentially growing cultures in starch medium. Immunoprecipitation data indicate that the abundance of alpha-amylase transcripts decreases dramatically after the first 12 h, reflecting an initial transcription control for the expression of this enzyme.Entities:
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Year: 1984 PMID: 6208985 DOI: 10.1139/o84-089
Source DB: PubMed Journal: Can J Biochem Cell Biol ISSN: 0714-7511