Preparation, analysis and $sup 15$N-NMR of $sup 15$N-labelled biological molecules
- eds.
From 1st international conference on stable isotopes in chemistry, biology, and medicine; Argonne, Illinois, USA (9 May l973). In proceedings of the first international conference on stable isotopes in chemistry, biology, and medicine. The application of total capability isotope research facilities to the preparation, analysis, and physical studies of /sup 15/N-labelled biological molecules is discussed, taking the preparation of /sup 15/Nhemoglobin (/sup 15/N > 50%) as an example. Strategies for biosynthesis of highly isotopically enriched proteins and enzymes are presented, with particular attention being given to a comparison in terms of yield and economy between the use of whole animals, tissue cultures and cell-free systems, the use of algal amino acid mixture as the /sup 15/N source, and the application of glc-mass fragmentography for the determination of the isotope enrichment of various amino acid groups in a labeled macromoIecule. The Fast Fourier Transform /sup 15/N--NMR spectra of several biologically interesting molecules is presented to demonstrate the potential of /sup 15/N--NMR. These include (a) an algal amino acid mixture, which demonstrates the resolving power of /sup 15/N--NMR, (b) pigment mixture, the first /sup 15/N--NMR of chlorophylls, (c) glycine and glycyglycine, which demonstrates the ability of /sup 15/N--NMR to determine subtle changes in the distribution of electron density in amino and peptide functional groups as function of pH, and (d) /sup 15/N-labelled macromolecules. (auth)
- Research Organization:
- Weizmann Inst. of Science, Rehovot, Israel; Argonne National Lab., Ill. (USA)
- NSA Number:
- NSA-29-000120
- OSTI ID:
- 4399481
- Report Number(s):
- CONF-730525--
- Country of Publication:
- Country unknown/Code not available
- Language:
- English
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