Trypsin und Erepsin.

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Calorimetry of some trypsin-trypsin inhibitor reactions.

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Trypsin Revisited

From the ‡European Molecular Biology Laboratory (EMBL) Hamburg c/o DESY, D-22607 Hamburg, Germany, the **Institute of Bioorganic Chemistry, Polish Academy of Sciences, 61–704 Poznan, Poland and Institute of Biochemistry and Molecular Biology, University Hospital, Hamburg-Eppendorf, c⁄o DESY, 22603 Hamburg, Germany, the ¶Laboratoire de Cristallographie et Modelisation des Matériaux Mineraux et B...

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Crystalline 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 ...

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Isolation from Beef Pancreas of Crystalline Trypsinogen, Trypsin, a Trypsin Inhibitor, and an Inhibitor-trypsin Compound

Methods are described for the isolation and crystallization of trypsinogen, trypsin, a substance which inhibits trypsin, and an inhibitor-trypsin compound. Analyses and some of the properties of these compounds are given.

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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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ژورنال

عنوان ژورنال: Hoppe-Seyler´s Zeitschrift für physiologische Chemie

سال: 1902

ISSN: 0018-4888

DOI: 10.1515/bchm2.1902.36.1.13