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Purification of an iron-binding nona-peptide from hydrolysates of porcine blood plasma protein

Paper ID Volume ID Publish Year Pages File Format Full-Text
35292 45084 2009 4 PDF Available
Title
Purification of an iron-binding nona-peptide from hydrolysates of porcine blood plasma protein
Abstract

To isolate a novel iron-binding peptide, porcine plasma protein (PPP) was hydrolyzed using a commercial protease. The degree of hydrolysis and iron-binding capacity was determined using the trinitrobenzenesulfonic acid and orthophenanthroline method, respectively. The hydrolysates of blood plasma protein were then filtered using YM-3 membrane, and an iron-binding peptide was isolated using gel permeation, ion exchange, and normal phase high-performance liquid chromatography. The purified iron-binding peptide was identified to be a nona-peptide, Asp–Leu–Gly–Glu–Gln–Tyr–Phe–Lys–Gly (1055 Da) based on liquid chromatography/electrospray ionization (LC/ESI) tandem mass spectrum and a sequence of porcine plasma protein.

Keywords
Blood plasma protein; Iron-binding peptide; Hydrolysates; Isolation
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Purification of an iron-binding nona-peptide from hydrolysates of porcine blood plasma protein
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Publisher
Database: Elsevier - ScienceDirect
Journal: Process Biochemistry - Volume 44, Issue 3, March 2009, Pages 378–381
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
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us