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温水鱼和冷水鱼胶原蛋白的水合作用与热力学研究。

A study of the hydration and thermodynamics of warm-water and cold-water fish collagens.

作者信息

Rose C, Kumar M, Mandal A B

机构信息

By-products Laboratory, Central Leather Research Institute, Adyar, Madras, India.

出版信息

Biochem J. 1988 Jan 1;249(1):127-33. doi: 10.1042/bj2490127.

Abstract

The hydrated volumes, Vh, of collagens extracted from various fish species were calculated by using the Simha-Einstein equation, and it was found that the hydration of warm-water fish collagen is greater than that of cold-water fish collagen (halibut). Although the intrinsic viscosities of warm-water fish (bigeye-tuna, carp and catfish) collagens are almost the same, the hydrated volume of bigeye-tuna collagen is approx. 1.5 and 3 times those of carp and catfish collagens respectively. The extent of hydration at 20 degrees C is in the following order: bigeye tuna greater than carp greater than catfish greater than halibut. The various thermodynamic activation parameters (delta G*, delta H* and delta S*) were calculated and it was found that they are useful for determining the exact denaturation temperature. It was calculated that the denaturation temperatures of halibut, bigeye-tuna, carp and catfish collagens are 17, 31, 32 and 26-30 degrees C respectively. The variations of hydration, intrinsic viscosity, denaturation temperature and the thermodynamic parameters with the variation of concentration of catfish collagen were also thoroughly examined. The change of thermodynamic parameters from coiled-coil to random-coil conformation upon denaturation of collagen were calculated from the amount of proline and hydroxyproline residues and compared with viscometric results.

摘要

利用辛哈 - 爱因斯坦方程计算了从各种鱼类中提取的胶原蛋白的水合体积(V_h),发现温水鱼胶原蛋白的水合作用大于冷水鱼(大比目鱼)胶原蛋白。尽管温水鱼(大眼金枪鱼、鲤鱼和鲶鱼)胶原蛋白的特性粘度几乎相同,但大眼金枪鱼胶原蛋白的水合体积分别约为鲤鱼和鲶鱼胶原蛋白的1.5倍和3倍。在20摄氏度时的水合程度顺序如下:大眼金枪鱼>鲤鱼>鲶鱼>大比目鱼。计算了各种热力学活化参数((\Delta G^)、(\Delta H^)和(\Delta S^*)),发现它们有助于确定确切的变性温度。经计算,大比目鱼、大眼金枪鱼、鲤鱼和鲶鱼胶原蛋白的变性温度分别为17、31、32和26 - 30摄氏度。还全面研究了鲶鱼胶原蛋白的水合作用、特性粘度、变性温度和热力学参数随浓度变化的情况。根据脯氨酸和羟脯氨酸残基的数量计算了胶原蛋白变性时从卷曲螺旋构象到无规卷曲构象的热力学参数变化,并与粘度测量结果进行了比较。

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