THE EQUILIBRIUM BETWEEN ACTIVE NATIVE TRYPSIN AND INACTIVE DENATURED TRYPSIN
نویسندگان
چکیده
منابع مشابه
The Equilibrium between Active Native Trypsin and Inactive Denatured Trypsin
There is a mobile equilibrium between the native and denatured forms of trypsin which depends on the concentrations of acid, alkali, and alcohol and on the temperature. The heat of denaturation in 0.01 N hydrochloric acid calculated from the effect of temperature on the equilibrium constant is -67,600 calories per mole.
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Inactive denatured trypsin changes into active native trypsin in the protein solutions which have been used to estimate tryptic activity. If the digestion mixture, however, is alkaline enough and contains enough urea this change does not take place. Such a digestion mixture can be used to estimate active native trypsin in the presence of inactive denatured trypsin.
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The effect of trypsin, chymotrypsin, and desoxyribonuclease on active, reversibly inactivated, and heat-inactivated B. megatherium phage, and on living and dead B. megatherium and B. coli has been determined. The results are summarized in Table I.
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Benzyl p-guanidinothiobenzoate hydrochloride was synthesized and demonstrated to be useful for active-site titration of bovine trypsin, bovine thrombin, human lung tryptase, bovine activated protein C, human Factor XIIa fragment and bovine Factor Xa beta. The titration is based on rapid formation of a stable acyl-enzyme with a stoichiometric release of benzyl thiol. Thiol production is measured...
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The denaturation of hemoglobin by salicylate in neutral solution is completely reversible. There is a mobile equilibrium between native and denatured hemoglobin in neutral salicylate solution. The higher the salicylate concentration the greater is the percentage denaturation. When there is a mobile equilibrium between the native and denatured forms of a protein, denaturation is caused by the ad...
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ژورنال
عنوان ژورنال: Journal of General Physiology
سال: 1934
ISSN: 1540-7748,0022-1295
DOI: 10.1085/jgp.17.3.393