. Aspects of the origin of life. Life; Biochemistry; Biochemistry; Biogenesis. 182 G. A. DEBORIN of the isotherms of trypsin compressibihty in a monolayer on 5% ammoniimi sulphate solution. Fig. i gives curves for the dependence of the surface pressure F on the product FA in a unimolecular layer for trypsin (curve I) and for the trypsin-ergosterol complex (curve II). These curves [26] indicate that the mole- cular weight of trypsin in the monolayer, as calculated according to the equation of ideal gases from the length of the section ^ between the intersections of the curves with the FA axis,
. Aspects of the origin of life. Life; Biochemistry; Biochemistry; Biogenesis. 182 G. A. DEBORIN of the isotherms of trypsin compressibihty in a monolayer on 5% ammoniimi sulphate solution. Fig. i gives curves for the dependence of the surface pressure F on the product FA in a unimolecular layer for trypsin (curve I) and for the trypsin-ergosterol complex (curve II). These curves [26] indicate that the mole- cular weight of trypsin in the monolayer, as calculated according to the equation of ideal gases from the length of the section ^ between the intersections of the curves with the FA axis, equals 40,000 for trypsin and 80,000 for its complex with ergosterol. Thus just as in the case of egg albumin, trypsin, in forming a complex with ergosterol, produces associates detectable in the monolayer. Special experiments revealed that this complex is maintained during 48 hours at a pH of 0-6 Fig. I. The dependence of the surface pressure F on the product FA in a monomolecular layer for trypsin (I) and for the trypsin-ergosterol complex (II). The proteolytic activity of trypsin was determined spectrophotometrically according to the Kunitz method [27] at 280 mju, and according to a modified Kunitz method at 400 m/x, as well as by determining the amino nitrogen in the incubated sample according to Van Slyke's method after precipitation by tri- chloroacetic acid. Fig. 2 gives curves for the digestion of serum albumin by trypsin (curve I) and by the trypsin—ergosterol complex (curve II) as a function of the amount of enzyme. Here the extinction at 280 m/x is plotted against the enzyme-substrate ratio. It follows from these curves that the complex has a higher proteoljrtic activity than pure trypsin, especially at enzyme/substrate ratios within the range T/200-1/50. Table i hsts the results of another experiment. In this case the optical densities (AEi for trypsin and for the complex) are obtained by subtracting the optical density after 90 minutes of proteolys
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