Functional properties of the acidic and basic subunits of the glycinin (11S) soy protein fraction
β Scribed by Kalyani Dias; Deland J. Myers; Yilin Bian; Makuba A. Lihono; Shaowen Wu; Patricia A. Murphy
- Publisher
- Springer-Verlag
- Year
- 2003
- Tongue
- English
- Weight
- 353 KB
- Volume
- 80
- Category
- Article
- ISSN
- 0003-021X
No coin nor oath required. For personal study only.
π SIMILAR VOLUMES
The functional properties of globin protein obtained from decolorisation of red cells of bovine blood were studied over a pH range of 2 to 12. Maximum foam stability and capacity were observed at pH 10 and buffer capacity at pH 2 and pH 11. In the range of pH 6Β±8, the globin protein showed an interm
The influence of acylation on surface functional properties, solubility and heat-induced aggregation of the low-molecular weight basic protein fraction (napin) from rapeseed was studied. While the native protein was soluble over the whole pH-range, the exhaustively acetylated one became precipitable
## The vertebrate Y-box proteins Structure and nucleic acid recognition The eukaryotic Y-box proteins were initially characterized through their interaction with duplex DNA containing the sequence CAAT('-7). The deduced amino acid sequence for the vertebrate proteins revealed an almost identically