| Literature DB >> 10190978 |
M A Kersten1, J J Baars, H J Op den Camp, L J Van Griensven, C van der Drift.
Abstract
The regulation of glutamine synthetase (GS) from Agaricus bisporus was studied at the posttranscriptional level using a specific antibody fraction directed against purified GS. The cross-reactivity of the antiserum against various Agaricus species and other fungi was tested and low reactivity with the Ascomycetes was found. GS protein and activity levels were measured in cell-free extracts of mycelium grown on different N sources. In mycelium grown on glutamine or ammonium as N source, the biosynthetic GS activity is higher than the transferase activity. Moreover, the results show a correlation between GS biosynthetic activity, GS protein, and previously reported mRNA levels. Also, after addition of ammonium or glutamine to glutamate-utilizing cultures, transferase activity decreased more rapidly than biosynthetic activity and GS protein level. This suggests a conformational modification which only affects transferase activity. Copyright 1999 Academic Press.Entities:
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Year: 1999 PMID: 10190978 DOI: 10.1006/abbi.1999.1119
Source DB: PubMed Journal: Arch Biochem Biophys ISSN: 0003-9861 Impact factor: 4.013