Archive image from page 300 of Currents in biochemical research, 1956;. Currents in biochemical research, 1956; twenty-seven essays charting the present course of biochemical research and considering the intimate relationship of biochemistry to medicine, physiology, and biology currentsinbioche1956gree Year: 1956 ( PROSTHETIC GROUPS, COENZYMES AND ENZYMES 2 3 4 5 6 7 8 9 10 11 12 Val-Glu(NH.)-Lys-Cy-Ala-Glu()-Cy-His-Thr-Val-Glu-Lys ! i S hematin S Interestingly enough the hemopeptides from cytochromes c of horse, beef, and pig had the same structure. In this part of the molecule near the
Archive image from page 300 of Currents in biochemical research, 1956;. Currents in biochemical research, 1956; twenty-seven essays charting the present course of biochemical research and considering the intimate relationship of biochemistry to medicine, physiology, and biology currentsinbioche1956gree Year: 1956 ( PROSTHETIC GROUPS, COENZYMES AND ENZYMES 2 3 4 5 6 7 8 9 10 11 12 Val-Glu(NH.)-Lys-Cy-Ala-Glu()-Cy-His-Thr-Val-Glu-Lys ! i S hematin S Interestingly enough the hemopeptides from cytochromes c of horse, beef, and pig had the same structure. In this part of the molecule near the prosthetic group, therefore, the cytochromes c from these different sources are identical, though species differ- ences may of course occur in other parts of the molecule. Since Paleus, working in this institute, had produced pure peptic degradation products of the cytochromes c from beef, chicken, and salmon, Tuppy came to Stockholm for some time to continue his research with Paleus (31). These peptic hemopeptides were considerably purer than Tsou's. The iron content was , and there were 20 nitrogen atoms per one Fe. The position of two additional amino acids in the molecule was established, and the sequence of aiTiino acids in the immediate vicinity of the prosthetic group in the case of beef and salmon cytochromes c can now be con- fidently asserted to be: 12 3456 789 10 11 12 —\'al-Glu(NH2)-Lys-Cy-Ala-Glu(NH2}-Cy-His-Thr-\-al-Glu-Lys The chicken cytochrome c showed a remarkable difference from the other ones; it contained serine in the place of alanine at position 5. The presence of a polar hydroxymethyl group instead of the nonpolar methyl group of alanine so close to the prosthetic group might be of functional importance, apart from the interesting example that it provides of a species difference. Since two amino acids are interposed between the two heme- 279
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