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Diluted aqueous solutions of some proteins (bovine serum albumin, β-Lactoglobubin, Peroxidase) show weak phosphorescence lasting over several minutes after they have been irradiated with light in the range 3500-4200 A. Addition of Eosin after the irradiation amplifies in some cases the intensity of luminescence to a value of about hundred. If Eosin is present at the irradiation process the excitation to phosphorescence is possible with light of the wavelength 5460 A.
After denaturation processes which destroy the configuration of proteins (Urea, Guanidine-HCI. detergents, heat at higher pH) the ability of phosphorescence disappears altogether; likewise after blocking the SH-groups by benzochinone or a total oxidation or reduction of the SS-groups which causes an complete unfolding of the peptide chain.
In solutions of bovine serum-albumin irradiated with 3650 Å at room temperature and afterwards frozen to -178°C no radicals could be observed by measurements of electron-spin-resonance but they were detectable if the irradiation took place in the presence of H2O2.
The reactions Xanthinoxidase-Xanthine-O2, Peroxidase-H2O2 and bovine serum-albumin-H2O2-Fe (II) EDTA are accompanied by chemiluminescence. By comparison with the behaviour of oxidised serum-albumin it could be shown that the chemical reaction produces an excited state of the native protein.
The observations lead to the conclusion that the weak phosphorescence of long duration originates from a triplet-state which is sufficiently populated only as the consequence of cooperative phenomena attending the undisturbed α-Helix-structure of the protein.
The two-nucleon potential is assumed to be a quadratic function of momentum: ν = ν1 (r) + pν2(r)p. The BETHE-GOLDSTONE equation (l = 0) has been solved for two different choices of ν. An analytical, approximate solution is obtained.
A study on the effect of UV-irradiated polyuridylic acid on the incorporation of phenylalanine into the polypeptide precipitable through trichloroacetic acid, in a cell-free system from E. coli was made. Attempts were made to reactivate the UV-inactivated polyuridylic acid through hydrogen peroxide, uranyl acetate and visible light. We could show that polyuridylic acid irradiated at a dose of 1.2 ×105 ergs/mm2 could be completely reactivated, while the one irradiated at a higher dose of 2.4 ×105 ergs/mm2 could not be completely reactivated under the conditions of our experiment. We have studied the effects of hydrogen peroxide and uranyl acetate on UV-irradiated polyuridylic acid chemically as well. Our results altogether show that the photoreactivating effect of uranyl acetate and hydrogen peroxide is due to their ability to split the uracil dimers formed during UV-irradiation.
Unter dem synergistischen Einfluß zweier Bakterien-Stämme, eines aeroben Sporenbildners (Bac. alvei) und eines Enterococcen-Stammes (Diplococcus I) wird Tropin vollständig in Pseudotropin umgewandelt. Der Mechanismus dieser trans-cis-Umlagerung wird diskutiert.
Zur Trennung von Tropan-Alkaloiden und deren Derivate werden geeignete chromatographische Laufmittelsysteme angegeben.
The kinetic data of the hydrolysis of some serine peptides in diluted hydrochloric acid and in pure water and of the rearrangement of O-glycyl-DL-serine to glycyl-DL-serine were determined.
The hydrolysis of glycyl-DL-serine and DL-alanyl-DL-serine proceeds surprisingly rapidly in pure water as compared with the hydrolysis of those peptides in 0.5 N hydrochloric acid as well as the hydrolysis of glycyl-DL-alanine in purely aqueous solution. The O → N migration of the glycyl residue in O-glycyl-DL-serine which probably is an intermediate in the cleavage of glycyl-DL-serine in purely aqueous solution represents a three center reaction in which the nucleophilic attack on the O-peptide and peptide bond, respectively, involves a free basic amino group. The analogy between the serine peptide interconversion and the hydrolysis catalyzed by certain proteolytic enzymes is referred to.
Under the conditions of freeze drying are formed in hydrochloric acid solutions of DL-alanyl-DL-serine O-peptide and depsipeptide.
Die kontinuierliche Messung des CO2-Gaswechsels homogener Sedimente einzelliger Grünalgen hat ergeben, daß das Kohlendioxyd während der ersten Belichtungsphase zunächst an einen primären, in den verdunkelten Zellen bereits vorhandenen CO2-Acceptor (AI) angelagert wird. AI ist nur im Licht zur Aufnahme und lockeren Bindung von Kohlendioxyd befähigt und gibt die während kurzer Lichtperioden (4-30 sec) aufgenommene CO2-Menge in der anschließenden Dunkelperiode sehr schnell wieder ab. Im Verlauf längerer Belichtungszeiten (> 30 sec) übergibt AI das locker gebundene Kohlendioxyd an den inzwischen in zunehmender Konzentration gebildeten CO2-Acceptor des Calvin - Zyklus (Ribulosediphosphat = AII). Die mit der Aufnahme und lockeren Bindung von Kohlendioxyd an den aktivierten Acceptor AI und der CO2-Weitergabe an AII zusammenhängenden Übergangserscheinungen werden eingehend diskutiert.