IDENTIFICATION OF THE TRYPSIN INHIBITOR OF EGG WHITE WITH OVOMUCOID
Journal of Biological Chemistry · 1947 · 281 citations · 28 references
Antiparasitic AgentImmunologyGlycobiologyDrug ResistanceBioanalysisClinical ChemistryEnzyme PrecursorsProteomicsInhibitory ActivityParasitologyAnimal PhysiologyAllergyBiochemistryActive Antitrypsin SamplePharmacologyNatural SciencesPathogenesisSulfur ContentMedicineDrug Discovery
The trypsin inhibiting action of egg white, which has been known for over 40 years, has not been identified with any of the recognized components (1) of egg white.Suggestions made in this regard include the postulates (a) that difficultly digestible proteins of egg white displaced trypsin from the substrate (casein) (2), (b) that the antitrypsin is associated with the globulin fraction of egg white (3), and (c) that the inhibitor is probably a protein hydrolysis product but not a true protein (4).Balls and Swenson (4), who made the most complete study of the inhibitor, found that it was neither lipide nor carbohydrate (exclusively) and that it had about the same nitrogen content (slightly low), optical rotation, and sulfur content as are now recognized for ovomucoid.Meyer et al. ( 5) reported that a highly active antitrypsin sample sent them by Dr. Swenson showed the properties and composition of an egg mucoid.They stated that '(the inhibitory effect of egg white preparations on tryptic activity is probably due to a mucoid."However, the activity reported by Balls and Swenson for their best preparation indicated that the inhibitor represented less than 1 per cent of the egg white solids, which, of course, is less than one-tenth of the ovomucoid in egg white.Possible explanation of this result, which conflicts with the results reported in this paper, may lie in the use for assay purposes of enzyme precursors, which were activated by enterokinase, generally in the presence of inhibitor.The complication introduced by the use of precursors and enterokinase (a common practice at the time the work was done) is illustrated by the reports that the inhibitor was an antikinase (6), that it possibly acted by displacing enterokinase from its combination with the enzyme (4), and that the inhibitor was not an antikinase (7, 2).This report concerns a component of egg white that inhibits trypsin containing no enterokinase.Primary consideration is given to data indicating that antitryptic activity is a characteristic of "native" ovomucoid.The considerations include the distribution of the inhibitor in hen's eggs, preparation and fractional precipitation of the inhibitor, comparison of the
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THE ESTIMATION OF PEPSIN, TRYPSIN, PAPAIN, AND CATHEPSIN WITH HEMOGLOBIN
M. L. Anson · The Journal of General Physiology · 1938
3.3K citations
ISOLATION FROM BEEF PANCREAS OF CRYSTALLINE TRYPSINOGEN, TRYPSIN, A TRYPSIN INHIBITOR, AND AN INHIBITOR-TRYPSIN COMPOUND
M. Kunitz, John H. Northrop · The Journal of General Physiology · 1936
Animal PhysiologyMedicinal ChemistryInhibitor-trypsin Compound+11
518 citations
ISOLATION OF LYSOZYME FROM EGG WHITE
Gordon Alderton, Wilfred H. Ward, H. L. Fevold · Journal of Biological Chemistry · 1945
279 citations
DIRECT CRYSTALLIZATION OF LYSOZYME FROM EGG WHITE AND SOME CRYSTALLINE SALTS OF LYSOZYME
Gordon Alderton, H. L. Fevold · Journal of Biological Chemistry · 1946
273 citations
Crystallization of a Trypsin Inhibitor from Soybean
M. Kunitz · Science · 1945
265 citations