Crystal Structure of Bis(cyclooctatetraene)titanium
β Scribed by Dr. H. Dietrich; M. Soltwisch
- Publisher
- John Wiley and Sons
- Year
- 1969
- Tongue
- English
- Weight
- 119 KB
- Volume
- 8
- Category
- Article
- ISSN
- 0044-8249
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β¦ Synopsis
The pentapeptide was electrophoretically and chromatographically homogeneous and on total hydrolysis gave the amino acids Phe. Glu, Gly. Leu, and Tyr in the proportions 0.98 : 1.13 : 1.00 : 1.07 : 0.89 (D. Georgopoulos). In the plastein reactionr31 with pepsin, a 25-mg sample gave 14 mg (60%) of water-insoluble polypeptide mixture. Paper electrophoresis at p H 6.5 separated the blocked intermediate peptides into the four expected constituents (2carboxy-3-nitrobenzoyl derivatives of Phe, Glu-Phe, Gly-Glu-Phe, and Leu-Gly-Glu-Phe), which appeared with approximately equal intensity on development with the tertbutyl hypochlorite-tolidine reagent 141.
π SIMILAR VOLUMES
estimated from the molecular volumes and data derived from a large amount of experimental material 121. In contrast, the considerably shorter relaxation time for triphenylamine can only be explained by internal mobility. Evidently inversion takes place, facilitated by the arrangement of the N-Ph bon