Inhibition of renal accumulation of lysozyme (basic low molecular weight protein) by basic proteins and other basic substances
β Scribed by C. Cojocel; M. Franzen-Sieveking; G. Beckmann; K. Baumann
- Publisher
- Springer
- Year
- 1981
- Tongue
- English
- Weight
- 625 KB
- Volume
- 390
- Category
- Article
- ISSN
- 0031-6768
No coin nor oath required. For personal study only.
π SIMILAR VOLUMES
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 binding of two differently substituted cellulose sulphates (CS) with DS 0.50 and 0.33 to two main rapeseed proteins, the high molecular mass neutral 12 S globulin and the low molecular mass basic protein fraction ("albumin") in insoluble complexes at pH < Pi (protein) has been studied using turb