Purification and partial characterisation of a novel trypsin-like cysteine protease fromMetarhizium anisopliae

Autor:	A. Keith Charnley, Stephen C.J. Cole, Richard M. Cooper
Rok vydání:	1993
Předmět:	Serine protease Proteases Protease biology medicine.medical_treatment Proteolytic enzymes Metarhizium anisopliae biology.organism_classification Trypsin Microbiology Cysteine protease Isoelectric point Biochemistry Genetics biology.protein medicine Molecular Biology medicine.drug
Zdroj:	FEMS Microbiology Letters. 113:189-195
ISSN:	1574-6968 0378-1097
DOI:	10.1111/j.1574-6968.1993.tb06512.x
Popis:	Trypsin-like enzymes from the entomopathogenic fungus Metarhizium anisopliae have been characterised. Two proteases with tryptic activity were purified by narrow range isoelectric focussing and affinity chromatography. One of these proteases, with an isoelectric point of 5.4 and a molecular mass of 28.8 kDa is a ‘classical’ trypsin belonging to the serine protease class. The other protease, with an isoelectric point of 4.6 and a molecular mass of 26.7 kDa, demonstrates trypsin-like specificity but, on the basis of inhibition and activation studies, belongs to the cysteine protease family and as such is the first fungal protease to be found of this type. The amino acid composition, kinetic constants and activity against proteinaceous substrates, including locust cuticle have been determined.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::91343c5a74db570272ef24a827836782 https://doi.org/10.1111/j.1574-6968.1993.tb06512.x Zobrazit plný text záznamu Plný text