Sood Satish M, Erickson Grant, Slattery Charles W
Department of Biochemistry and Microbiology, Biochemistry Division, , School of Medicine, Loma Linda University, Loma Linda, CA 92350, USA.
Protein J. 2005 May;24(4):227-32. doi: 10.1007/s10930-005-6715-2.
The beta-casein (CN) human milk fraction is comprised of a single protein phosphorylated at levels from 0 to 5. Component interactions are dependent on the phosphorylation level. Here, 3 mg/ml of beta-CN-0P, beta-CN-2P, beta-CN-4P, a 2P/4P 1:1 (wt:wt) mixture, or a mixture of all six forms in the ratio in human milk, were mixed with bovine kappa-CN at a kappa/beta molar ratio of 0.33. Measurements were with 0, 5 and 10 mM Ca+2 and 4 and 8 mM added inorganic phosphate (Pi). The turbidity (OD400 nm) and a lack of precipitation as T increased from 4 to 37 degrees C was an index of micelle formation. The results indicate: (1) while micelles will form with Ca+2 alone, added Pi has a significant enhancing effect on micelle formation; (2) the patterns of micelle formation as a function of T are influenced by the beta-CN-0P and beta-CN-1P forms of beta-CN to an unexpected extent.
β-酪蛋白(CN)人乳组分由一种磷酸化水平在0至5之间的单一蛋白质组成。组分间的相互作用取决于磷酸化水平。在此,将3mg/ml的β-CN-0P、β-CN-2P、β-CN-4P、2P/4P 1:1(重量比)混合物或六种形式按人乳比例混合的混合物,与κ-酪蛋白以κ/β摩尔比0.33混合。测量在添加0、5和10mM Ca²⁺以及4和8mM无机磷酸盐(Pi)的条件下进行。当温度从4℃升高到37℃时,浊度(OD400nm)和无沉淀现象是胶束形成的指标。结果表明:(1)虽然单独的Ca²⁺会形成胶束,但添加的Pi对胶束形成有显著的增强作用;(2)β-CN的β-CN-0P和β-CN-1P形式对胶束形成模式随温度变化的影响程度出乎意料。