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Purification and characterization of extracellular cysteine protease inhibitor, ECPI-2, from Chlorella sp.

Paper ID Volume ID Publish Year Pages File Format Full-Text
22381 43273 2006 6 PDF Available
Title
Purification and characterization of extracellular cysteine protease inhibitor, ECPI-2, from Chlorella sp.
Abstract

An extracellular cysteine protease inhibitor (ECPI-2) was purified to homogeneity from the culture filtrate of Chlorella sp. 4533 by the combination of various column chromatographies. The molecular mass of the inhibitor was estimated to be 340 kDa by SDS–PAGE. The inhibitor was extremely heat-stable under acidic or neutral condition. ECPI-2 exhibited an inhibitory activity against the proteolytic activity of papain, ficin, or chymopapain, but not against stem bromelain or cathepsin B. The inhibitor showed no inhibitory activity against trypsin, α-chymotrypsin or thermolysin. ECPI-2 contains 33.6% carbohydrate residues by weight and inhibits papain at a molar ratio of 1:2. The proteolysis of the inhibitor by trypsin or α-chymotrypsin was apparent, but the inhibitory activity of ECPI-2 was unaffected by these enzymes. The α-chymotrypsin hydrolysis product from ECPI-2 was further separated into six fractions by gel filtration. From these results, it is suggested that ECPI-2 has several reactive sites for papain.

Keywords
green alga; Chlorella; cysteine protease inhibitor; glycoprotein
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Purification and characterization of extracellular cysteine protease inhibitor, ECPI-2, from Chlorella sp.
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Bioscience and Bioengineering - Volume 101, Issue 2, February 2006, Pages 166–171
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
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Full-text PDF Download
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