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65A-12: Reductive alkylation of blood proteins

Nyman, RE, Nelson, G and Owusu-Apenten, R (1999) 65A-12: Reductive alkylation of blood proteins. In: 1999 IFT Annual Meeting, July 24 - 28, Chicago, IL. IFT. 1 pp. [Conference contribution]

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URL: http://ift.confex.com/ift/99annual/techprogram/abstracts/3497.htm

Abstract

Globin and plasma were chemically modified by reductive alkylation using 4-hydroxybenzaldehyde and the reducing agent sodium cyanoborohydride. The resulting derivatives were analysed to determine their solubility and protein concentration. The degree of modification was estimated by amino acid analysis and sodium dodecyl-sulphate polyacrylamide gel electrophoresis. The protein solutions were brought to neutrality with sodium hydroxide to allow optimum enzymatic cross-linking. RESULTS: The derivatives were found to be very insoluble at pH 6; optimum solubility (90-95%) was found at pH 2 and 60?C (pre-heating). The optimum pH values for tyrosinase-catalysed cross-linking of globin and plasma derivatives were 7 and 8, respectively. Kjeldhal nitrogen analysis resulted in estimates of the protein content of the derivatives at approximately 75%. Analysis of the derivatives proved that modification had occurred. Amino acid analysis determined that globin and plasma were 73% and 27% modified, respectively. Electrophoresis confirmed a qualitative increase in molecular weight. SIGNIFICANCE: Enzymatic cross-linking of proteins is an alternative and potentially less expensive method of gelation, carried out at low temperature compared to the traditional heat-induced method

Item Type:Conference contribution (Poster)
Faculties and Schools:Faculty of Life and Health Sciences > School of Biomedical Sciences
Faculty of Life and Health Sciences
Research Institutes and Groups:Biomedical Sciences Research Institute > Nutrition Innovation Centre for Food and Health (NICHE)
Biomedical Sciences Research Institute
ID Code:24453
Deposited By: Dr Richard Owusu-Apenten
Deposited On:09 Jan 2013 11:12
Last Modified:09 Jan 2013 11:12

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