Structural stability of globulins

被引：49

作者：

Gorinstein, S ^{[1
]}

Zemser, M ^{[1
]}

ParedesLopez, O ^{[1
]}

机构：

[1] IPN,CTR INVEST & ESTUDIOS AVANZADOS,DEPT BIOTECNOL & BIOQUIM,IRAPUATO 36500,GUANAJUATO,MEXICO

来源：

JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY | 1996年 / 44卷 / 01期

关键词：

amaranth; quinoa; calorimetry; denaturation; spectroscopy;

D O I：

10.1021/jf9500849

中图分类号：

S [农业科学];

学科分类号：

09 ;

摘要：

Application of differential scanning calorimetry (DSC) and the susceptibility of amaranth globulins (A-G) to alpha-chymotrypsin gave a quantitative estimation of protein denaturation in solid state. To compare effects of size and crystal structure, A-G, quinoa globulins (Q-G), and bovine gamma-globulins (gamma-G) were examined at similar conditions for the extent of denaturation. A-G and Q-C: showed similar data, but gamma-G exhibited maximal conformational changes, The larger percentage of denaturation in globulins that is associated with enthalpy and the number of ruptured hydrogen bonds correspond to the smaller crystallinity determined by X-ray diffraction and disappearance of the alpha-helix in Fourier transform-infrared spectre.

引用

页码：100 / 105

页数：6

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