Relationship between color development and protein conformation in the phycocyanin molecule
| Autor: | Yukinori Noguchi, Hiroyuki Nishimura, Yoh Kodera, Yuji Inada, Tetsuya Saito, Kouji Fukui, Ayako Matsushima |
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| Rok vydání: | 2004 |
| Předmět: |
chemistry.chemical_classification
Chemistry Stereochemistry Process Chemistry and Technology General Chemical Engineering Lysine Chemical modification macromolecular substances Absorbance chemistry.chemical_compound Protein structure Phycocyanobilin Phycocyanin Propionate Denaturation (biochemistry) |
| Zdroj: | Dyes and Pigments. 63:89-94 |
| ISSN: | 0143-7208 |
| Popis: | Phycocyanin with blue color, phycocyanobilin bound to protein, with the absorption maximum at 614 nm is quite unstable against urea-treatment because of the denaturation of the protein conformation. To prevent the bleaching of phycocyanin by urea, amino groups of lysine residues in the phycocyanin molecule were modified with DSP [dithiobis(succinimidyl propionate)] to cross-link amino groups in the protein molecule in order to maintain the high order structure of phycocyanin. The color development of DSP-modified phycocyanin became stable, but unmodified phycocyanin was markedly decreased to 20% of the original absorbance at 614 nm against urea-treatment. Splitting of the S–S linkage of DSP-modified phycocyanin molecule by 2-mercaptoethanol caused the reduction of color development of phycocyanin under urea-treatment. The color development of phycocyanin is closely associated with its high order structure of protein. |
| Databáze: | OpenAIRE |
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