Analysis of the protein pattern of Gremmeniella abietina with special reference to protease activity
Autor: | Raija-Liisa Petäistö, Rauno J. Harvima, T. E. Rissanen, E. O. Kajander |
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Rok vydání: | 1994 |
Předmět: |
0106 biological sciences
0301 basic medicine Proteases Physiology medicine.medical_treatment Fungus 010603 evolutionary biology 01 natural sciences Microbiology 03 medical and health sciences chemistry.chemical_compound Gremmeniella Genetics medicine Molecular Biology Ecology Evolution Behavior and Systematics Mycelium Scleroderris canker Fungal protein Protease biology Cell Biology General Medicine 030108 mycology & parasitology biology.organism_classification Biochemistry chemistry Pepstatin |
Zdroj: | Mycologia. 86:242-249 |
ISSN: | 1557-2536 0027-5514 |
DOI: | 10.1080/00275514.1994.12026401 |
Popis: | Gremmeniella abietina is the causative agent in Scleroderris canker of conifers. This fungus grows very slowly and thus its protein pattern may be difficult to obtain, especially since fungal protease activities are unknown. We show that the protease activity is very low in young cultures grown in Campbell's V8 juice liquid medium but degraded some of the protein bands making it very difficult to reliably compare electro? phoretic protein pattern from sample to sample. A calcium- and zinc-dependent metalloprotease activity was specifically detected, and it was inhibited by ethyl- enediaminetetraacetate and o-phenanthroline at a neutral pH. Other protease activities may be present since inhibition of the proteolytic activity by p-chlo- romercuribenzoate and pepstatin was also seen. Phen- ylmethanesulfonyl fluoride showed only minimal in? hibitory effect. The fungal protein patterns were reproducible with only small intensity differences be? tween different culture batches. The protein pattern resembled that of Sirococcus strobilinus, but immuno- blotting with anti-Gremmeniella antibody showed no cross-reactivity and thus Sirococcus may not be closely related to Gremmeniella. |
Databáze: | OpenAIRE |
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