Extracellular proteinases of Claviceps purpurea. Isolation and characterization of an aspartic proteinase View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1983-03

AUTHORS

Igor Kregar, Anka Puc, Vito Turk

ABSTRACT

An aspartic proteinase was isolated from the culture filtrate of Claviceps purpurea by a method which includes affinity chromatography on immobilized inhibitor pepstatin, gel filtration and ion-exchange chromatography. The isolated enzyme was electrophoretically homogenous, had a molecular weight between 41,000 and 43,000 and pI 4.60. It was most active toward hemoglobin at pH 3.5. The enzyme was unstable above pH 7. It was completely inhibited by pepstatin, whereas diazoacetyl norleucine methyl ester and epoxy(p-nitrophenoxy)propan inactivated the enzyme by 40%. More... »

PAGES

129-132

References to SciGraph publications

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/bf00499864

DOI

http://dx.doi.org/10.1007/bf00499864

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1028049127


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