منابع مشابه
The Sulfhydryl Groups of Egg Albumin
1. 1 cc. of 0.001 M ferricyanide, tetrathionate, or p-chloromercuribenzoate is required to abolish the SH groups of 10 mg. of denatured egg albumin in guanidine hydrochloride or Duponol PC solution. Both the nitroprusside test and the ferricyanide reduction test are used to show that the SH groups have been abolished. 2. 1 cc. of 0.001 M ferrocyanide is formed when ferricyanide is added to 10 m...
متن کاملSulfhydryl Groups in Films of Egg Albumin
1. The same number of SH groups reduces ferricyanide in surface films of egg albumin as in albumin denatured by urea, guanidine hydrochloride, Duponol, or heat, provided the ferricyanide reacts with films while they still are at the surface and with the denatured proteins while the denaturing agent (urea, heat, etc.) is present. 2. The SH groups of a suspension of egg albumin made by clumping t...
متن کاملSulfhydryl Groups of Egg Albumin in Different Denaturing Agents
1. The reaction between ferricyanide and egg albumin in solutions of urea, guanidine hydrochloride, and Duponol has been investigated. 2. In neutral medium ferricyanide oxidizes all the SH groups of egg albumin that give a color reaction with nitroprusside. In neutral medium ferricyanide appears to react only with the SH groups of egg albumin. The quantity of ferrocyanide formed can accordingly...
متن کاملSulfhydryl Groups in Proteins Iii. the Effect on Egg Albumin of Various Salts of Guanidine by Jesse P. Greenstein
The denaturation of certain proteins is characterized in part by the appearance of titratable sulfhydryl groups (8,11, 13).’ Moreover, the proportion of these groups which appears in any one protein is dependent upon the method of denaturation employed (3,5,6). Proteins dissolved in solutions of urea, guanidine hydrochloride, and related substances show widely different amounts of sulfhydryl gr...
متن کاملSulfhydryl Groups in Proteins Iii. the Effect on Egg Albumin of Various Salts of Guanidine by Jesse
The denaturation of certain proteins is characterized in part by the appearance of titratable sulfhydryl groups (8,11, 13).’ Moreover, the proportion of these groups which appears in any one protein is dependent upon the method of denaturation employed (3,5,6). Proteins dissolved in solutions of urea, guanidine hydrochloride, and related substances show widely different amounts of sulfhydryl gr...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Journal of General Physiology
سال: 1941
ISSN: 1540-7748,0022-1295
DOI: 10.1085/jgp.24.4.399