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Purification and characterization of a new fungalysin-like metallopeptidase from the culture filtrate of a plant worm, Nomuraea atypicola

Paper ID Volume ID Publish Year Pages File Format Full-Text
34864 45052 2013 5 PDF Available
Title
Purification and characterization of a new fungalysin-like metallopeptidase from the culture filtrate of a plant worm, Nomuraea atypicola
Abstract

A new protease was purified from the culture filtrate of a plant worm, Nomuraea atypicola. The activity of the protease was suppressed by metalloprotease inhibitors such as EDTA and 1,10-phenanthroline, suggesting that it might be a metalloprotease. Its molecular mass was estimated to be 48 kDa by SDS-PAGE, and its optimal pH and temperature were pH 8.5–9.0 and 40 °C, respectively. The N-terminal amino acid sequence of the metalloprotease was similar to those of fungalysin metallopeptidases of the M36 family from fungi such as Coccidioides posadasii, Pyrenophora tritici-repentis, and Arthroderma gypseum, supporting the idea that it is a fungalysin-like metallopeptidase.

► A new protease was purified from the culture filtrate of a plant worm, Nomuraea atypicola. ► The activity of the protease was suppressed by several known metalloprotease inhibitors. ► The N-terminal amino acid sequence of the N. atypicola protease was similar to those of fungalysin metallopeptidases of the M36 family from fungi.

Keywords
Metallopeptidase; Fungalysin; Nomuraea atypicola
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Purification and characterization of a new fungalysin-like metallopeptidase from the culture filtrate of a plant worm, Nomuraea atypicola
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Publisher
Database: Elsevier - ScienceDirect
Journal: Process Biochemistry - Volume 48, Issue 1, January 2013, Pages 190–194
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
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Price was $35.95
You save - $31
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Full-text PDF Download
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Any Questions? feel free to contact us