PROTEOLYTIC ENZYMES
Open Access
- 20 March 1946
- journal article
- research article
- Published by Rockefeller University Press in The Journal of general physiology
- Vol. 29 (4) , 219-247
- https://doi.org/10.1085/jgp.29.4.219
Abstract
1. The literature on conditions affecting the activity of proteolytic enzymes has been reviewed. 2. Experimental data on the control of the activity of trypsin, leucoprotease, papain, serum antiprotease, leucopeptidase, and pancreatic peptidase have been presented. These data indicate that: (a) The polymorphonuclearleucocytes of the cat contain abundant proteinase and peptidase active at neutral pH; those of the rabbit lack proteinase active at neutral pH. (b) Reducing agents, including several biologically important thiol-sulfhydryl compounds and ascorbic acid, inhibit the activity of leucoprotease and trypsin. For each reductant the degree of inhibition is proportional to the reducing capacity of the medium. (c) p-Aminobenzoic acid, sulfonamides (especially sulfathiazole), and many diphenyl sulfones inhibit the activity of leucoprotease. (d) Serum, plasma, several heavy metals, ammonium salts, asparagine, thiourea, heparin, glutamic acid, tyrothricin, calcium chloride, and bile salts and bile acids also inhibit the activity of leucoprotease, and in most cases of trypsin too. (e) Preparations of tryptic digests of proteins, and egg white trypsin inhibitor, inhibit trypsin to a much greater degree than leucoprotease. (f) Mild oxidizing agents increase the activity of leucoprotease and trypsin. (g) Oxidizing agents and some inhibitors of sulfhydryl groups inhibit the antiproteolytic activity of the serum. It is suggested that serum antiprotease may consist (chiefly) of reducing agents, including thiol-sulfhydryl peptides which exert their antiproteolytic activity by virtue of the presence of sulfhydryl groups. (h) The antiproteolytic activity of the serum is progressively weakened by exposure to a hydrogen ion concentration below pH 6.5 or above pH 9.7. Because of this the pH optima of leucoprotease and trypsin are shifted in the presence of serum from pH of 7 and 8 to pH of 6 to 6.5, and the range of activity of these enzymes is slightly widened, in both acid and alkaline reactions. (i) Reducing agents increase the activity of leucopeptidase and pancreatic peptidase. Serum, sulfathiazole, and thiourea have little or no effect. 3. The significance of the oxidation-reduction system in the control of the activity of leucoprotease, trypsin, serum antiprotease, leucopeptidase, and pancreatic peptidase has been emphasized.This publication has 19 references indexed in Scilit:
- o-Iodosobenzoic Acid, a Reagent for the Estimation of Cysteine, Glutathione, and the Substituent Sulfhydryl Groups of Certain Proteins1Journal of the American Chemical Society, 1941
- Studies on the proteinases of some anaerobic and aerobic micro-organismsBiochemical Journal, 1939
- Über den Trypsin-Inhibitor des Blutes. Dritte Mitteilung zur Kenntnis des Plasmatrypsinsystems.Hoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1938
- The effect of halogen salts on tryptic digestionBiochemical Journal, 1933
- Über die Einwirkung von Oxydations- und Reduktionsmitteln auf Papain. II. Die Aktivitätsbeeinflussung durch Licht, Organoarsenverbindungen und Ascorbinsäure.Hoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1933
- Über den Einfluß von Oxydations- und Reduktionsmitteln auf die Aktivität von Papain.Hoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1933
- Über die Aktivierung tierischer und pflanzlicher Proteasen durch Glutathion. 16. Abhandlung über Pflanzenproteasen in der von R. Willstätter und Mitarbeitern begonnenen Untersuchungsreihe.Hoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1931
- Über natürliche Aktivatoren und Hemmungskörper proteolytischer Enzyme.Hoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1930
- The reaction of azine compounds with proteolytic enzymesBiochemical Journal, 1929
- THE EFFECT OF OXIDATION OF FILTRATES OF A CHICKEN SARCOMA (CHICKEN TUMOR I—ROUS)The Journal of Experimental Medicine, 1928