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Danielsson B, Mosbach K (1988) Methods Enzymol 137:181 4. Mosbach K, Danielsson B (1974) Biochim Biophys Acta 364:140 5. Weaver JC, Cooney CL, Fulton SP, Schuler D, Tannenbaum SR (1976) Biochim Biophys Acta 452:285 6. Pennington SN (1976) Anal Biochem 72:230 7. Tran-Minh C, Vallin D (1978) Anal Chem 50:1874 8. Rich S, Ianiello RM, Jesperson ND (1979) Anal Chem 51(2):204 9. Bowers LD, Carr PW (1976) Clin Chem 22:1427 10. Schmidt H-L, Krisam G, Grenner G (1976) Biochim Biophys Acta 429:283 11. Kiba N, Tomiyasu T, Furusawa M (1984) Talanta 31:131 12.

14. On-line-data of a hemodialysis experiment 56 F. Lammers · Th. Scheper time measurements at hospitals. Moreover, patients individual urea level and ureases long term stability encourages one to employ the method in routine treatment. 4 Kinetic Characterization of Immobilized Biocatalysts Immobilized enzymes are not restricted to bioanalytical applications. Increasingly they attract a huge amount of interest in industrial organic chemistry due to their excellent stereo- and enantioselectivity.

Here, medium concentrations up to 10 g/l are used (Amici et al. 1967). The ET is set up for L-asparagine analysis by columns of immobilized aparagine (200 units). 5 and 100 mmol/l. 6. 05 M Tris/HCl as well. The latter might be interesting for samples with high magnesium content. In this case, potassium phosphate buffer is not suitable because magnesium phosphate causes problems in FIA-systems. Especially in mammalian cell cultivations, the aminoacid L-glutamine and glucose represent the most important energy sources.

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