Reversible inactivation of trypsin by anhydrous formic acid.
Reversible inactivation of trypsin by anhydrous formic acid.
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无水甲酸可逆地灭活胰蛋白酶。
DOI：
10.1016/s0021-9258(18)70304-9
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发表时间：
1959
期刊：
影响因子：
--
通讯作者：
H. Neurath
中科院分区：
文献类型：
--
作者：
L. Smillie;H. Neurath
材料和方法-以胰酶原为原料，通过Pecher和Neurath(5)的快速活化法制备胰酶。“1998年胰酶原(地段编号TG 522)是由新泽西州弗里霍尔德的沃辛顿生化公司制备的一次结晶并含有50%MgS04的产品。将该蛋白溶解于0.01M的盐酸中，在0.001 M的盐溶液中进行广泛的冷透析，pH为3.0，然后冷冻干燥。活化液经胰酶活化后，用0.001 MHCl透析，冷冻干燥。以Baker和Adamson(98%~100%)产品为原料，用硼酸酐干燥制得无水甲酸
Materials and Methods-Trypsin was prepared from trypsinogen by the rapid activation procedure of Pechere and Neurath (5). Trypsinogen (Lot No. TG 522) was a product, crystallized once, and containing 50 per cent MgS04, prepared by the Worthington Biochemical Corporation, Freehold, New Jersey. The protein was dissolved in 0.01 M HCl, dialyzed extensively in the cold against 0.001 M HCl, pH 3.0, and lyophilized. After activation to trypsin, the activation mixture was dialyzed against 0.001 M HCl and lyophilized. Anhydrous formic acid was prepared by drying the Baker and Adamson (98 to 100 per cent) product over boric anhydride