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The role of pH and its control on effective conjugation of bovine hemoglobin and human serum albumin

Paper ID Volume ID Publish Year Pages File Format Full-Text
36124 45122 2007 7 PDF Available
Title
The role of pH and its control on effective conjugation of bovine hemoglobin and human serum albumin
Abstract

Human serum albumin (HSA) and bovine hemoglobin (Hb) conjugate is a promising candidate as a blood substitute. However, preparation of the conjugate is problematic because both proteins tend to conjugate between themselves rather than crosslink each other. In this work, a facile process for conjugation of Hb and HSA was developed through control strategy of the reaction. The reaction was carried out in a buffer containing borax-borate and mannite. The borax-borate was used for pH buffering while mannite was used as a pH switch and a reaction promoter. As a result, self-conjugation of Hb and self-conjugation of HSA were minimized. After the one-step conjugation reaction in aqueous solution, followed by the one-step purification by ion-exchange chromatography, the conjugate of HSA and Hb was obtained with the total yield about 50%. The P50 and the Hill coefficient for the product were 16.1 mmHg and 1.82, respectively.

Keywords
Human serum albumin (HSA); Bovine hemoglobin (Hb); Borax-borate buffer–mannite system; Conjugate; Blood substitute
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The role of pH and its control on effective conjugation of bovine hemoglobin and human serum albumin
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Publisher
Database: Elsevier - ScienceDirect
Journal: Process Biochemistry - Volume 42, Issue 3, March 2007, Pages 303–309
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