Reversible Inactivation of Trypsin by Anhydrous Formic Acid
نویسندگان
چکیده
منابع مشابه
Reversible inactivation of trypsin by anhydrous formic acid.
The inactivation of lysozyme and ribonuclease by anhydrous formic acid has been shown by Josefsson and Edman (1, 2) to be reversed by adjustment of an aqueous solution of the inactivated enzyme to pH 6.0 to 8.5. Reactivation was accompanied by an uptake of base, approximately equivalent to the number of serine and threonine residues in the proteins. With both proteins an increase in the positiv...
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General aspects of the mechanism of antithrombin action were elucidated by a comparison of the inactivation of trypsin by antithrombin with the inactivation of coagulation proteinases by the inhibitor. Bovine antithrombin and bovine trypsin were shown to form an inactive equimolar complex. A non-complexed, proteolytically modified form of antithrombin, electrophoretically identical with that fo...
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1. The inactivating effect of soft x-rays on trypsin in solutions of various degrees of concentration has been studied. 2. It has been found to run parallel with spontaneous heat inactivation. It is almost, if not entirely, confined to the free or active trypsin. 3. Under radiation of constant intensity, the inactivation follows the simple exponential law which indicates a monomolecular reactio...
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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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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 ...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1959
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)70304-9