酪蛋白胶束的核磁共振氢谱研究。
A 1H-n.m.r. study of casein micelles.
作者信息
Griffin M C, Roberts G C
出版信息
Biochem J. 1985 May 15;228(1):273-6. doi: 10.1042/bj2280273.
The 1H-n.m.r. spectrum of casein micelles consists of a small number of moderately sharp (linewidth approx. 60 Hz) resonances superimposed on the envelope of very broad lines expected for particles of this size. These sharp lines resemble, in chemical shift and relative intensity, the spectrum of the isolated 'macropeptide' released from the micelles by treatment with chymosin. The sharp lines in the casein micelle spectrum are further sharpened by addition of chymosin and broadened markedly by addition of ethanol. These observations are consistent with the proposal that the 'macropeptide' (the C-terminal 64 residues of K-casein) forms flexible 'hairs' on the surface of the micelles.
酪蛋白胶束的¹H-核磁共振谱由少量中等尖锐（线宽约60赫兹）的共振峰叠加在这种尺寸颗粒预期的非常宽的谱线包络上组成。这些尖锐的谱线在化学位移和相对强度方面类似于通过用凝乳酶处理从胶束中释放出的分离“大肽”的谱图。酪蛋白胶束谱中的尖锐谱线通过添加凝乳酶进一步锐化，并通过添加乙醇显著变宽。这些观察结果与“大肽”（κ-酪蛋白的C末端64个残基）在胶束表面形成柔性“毛发”的提议一致。
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