INACTIVATION OF CRYSTALLINE TRYPSIN
نویسندگان
چکیده
منابع مشابه
Inactivation of Crystalline Trypsin
1. The rate of inactivation of crystalline trypsin solutions and the nature of the products formed during the inactivation at various pH at temperatures below 37 degrees C. have been studied. 2. The inactivation may be reversible or irreversible. Reversible inactivation is accompanied by the formation of reversibly denatured protein. This denatured protein exists in equilibrium with the native ...
متن کاملA Photochemical Yield for the Inactivation of Crystalline Trypsin
That enzymes can be inactivated by exposure to ultraviolet light has been demonstrated qualitatively by a number of investigators (l), but very few experiments have been conducted under conditions which permitted a calculation of the number of molecules inactivated per quantum of radiation absorbed. Obviously data of the latter type can be secured only for pure enzymes whose molecular weight is...
متن کاملCrystalline Trypsin Iv. Reversibility of the Inactivation and Denaturation of Trypsin by Heat
I t was noted by Mellanby and Wooley (1) that trypsin solutions in dilute acid could be heated nearly to boiling with very little loss in activity, and this observation was confirmed by Eddie (2). At temperatures below 40°C., on the other hand, the enzyme is more stable near pH 4 or 5 than it is in acid solution. This latter result has also been obtained by the writer (3) and by Pace (4). In th...
متن کاملCrystalline Trypsin
A method is described for isolating a crystalline protein of high tryptic activity from beef pancreas. The protein has constant proteolytic activity and optical activity under various conditions and no indication of further fractionation could be obtained. The loss in activity corresponds to the decrease in native protein when the protein is denatured by heat, digested by pepsin, or hydrolyzed ...
متن کاملThe Inactivation of Trypsin
1. A study has been made of the equilibrium existing between trypsin and the substances formed in the digestion of proteins which inhibit its action. 2. This substance could not be obtained by the hydrolysis of the proteins by acid or alkali. It is dialyzable. 3. The equilibrium between this substance (inhibitor) and trypsin is found to agree with the equation, trypsin + inhibitor right harpoon...
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ژورنال
عنوان ژورنال: Journal of General Physiology
سال: 1934
ISSN: 1540-7748,0022-1295
DOI: 10.1085/jgp.17.4.591