Conservative chemical modification of proteins to study the effects of a single protein property on partitioning in aqueous two-phase systems

Biotechnology and Bioengineering

Volumn 49, Issue 3, 1996, Pages 290-299

  Franco, T T ^a,b   Andrews, A T ^a   Asenjo, J A ^a,c  

^a UNIVERSITY OF READING   (United Kingdom)

^b UNIVERSITY OF CAMPINAS   (Brazil)

^c UNIVERSITY OF CHILE   (Chile)

Author keywords

lactoglobulin; BSA; partitioning in aqueous system; proteins, modified; thaumatin

Indexed keywords

ACYLATION; BINARY MIXTURES; CHEMICAL MODIFICATION; MOLECULAR WEIGHT; ORGANIC ACIDS; PURIFICATION; SURFACE PHENOMENA; SURFACE PROPERTIES;

AMINO GROUPS; ANHYDRIDES; AQUEOUS TWO PHASE SYSTEMS; HYDROPHOBICITY; ISOELECTRIC POINTS; PARTITIONING; THAUMATIN;

PROTEINS;

BETA LACTOGLOBULIN; BOVINE SERUM ALBUMIN; THAUMATIN;

ACYLATION; AQUEOUS SOLUTION; ARTICLE; CHEMICAL MODIFICATION; ENZYME MECHANISM; GENETIC CONSERVATION; HYDROPHOBICITY; NONHUMAN; PARTITION COEFFICIENT; PROTEIN METABOLISM; PROTEIN MODIFICATION; STRUCTURE ACTIVITY RELATION; SURFACE PROPERTY;

BOVINAE;

EID: 0030569902     PISSN: 00063592     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0290(19960205)49:3<290::AID-BIT7>3.0.CO;2-F     Document Type: Article

References (27)

1. Albertsson, P.-A. 1971. Partition of cell particles and macromolecules. 2nd edition. Wiley, New York.
2. Albertsson, P.-A. 1986. Partition of cell particles and macromolecules. 3rd edition. Wiley, New York.
3. Alvaro, G., Russel, A. J. 1991. Modification of enzyme catalysis by engineering surface charge. In: J. J. Langone (ed.), Methods in enzymology, molecular design and models, vol. 202. Academic Press, San Diego, CA.
4. Andrews, A. T. 1986. Electrophoresis: Theory, techniques and biological and clinical applications. 2nd edition. Oxford University Press, Oxford.
5. Asenjo, J. A., Franco, T. T., Andrews, A. T., Andrews, B A. 1990. Affinity separation of proteins in aqueous two-phase systems, pp. 439-454. In: M White S Reuveny, and S. Shafferman (eds.), Biologicals from recombinant microorganisms and animal cells - new strategies in production and recovery. VCH, Mannheim.
6. Brooks, D. E., Sharp, K. A., Fisher, D. 1985. Theoretical aspects of partitioning. In: H. Walter, D. E. Brooks, and D. Fisher (eds.), Partition in two aqueous phase systems. Academic Press, New York.
7. Butler, P. J. G., Harris, J. I., Hartley, B. S., Leberman R. 1969. Use of maleic anhydride for the reversible blocking of amino groups in polypeptide chains. Biochem. J. 112: 679.
8. Cascone, O., Andrews, B. A., Asenjo, J. A. 1991. Partitioning and purification of thaumatin in aqueous two-phase systems. Enz. Microb. Technol. 13: 629-635.
9. Deutscher, M. P. 1990. Maintaining protein stability, in: M. P. Deutscher (ed.). Methods in enzymology. Guide to protein purification. Academic Press, San Diego, CA.
10. Franco, T. T., Andrews, B. A., Cascone, O., Hodgson, C., Andrews, A. T., Asenjo, J. A. 1990. pp. 335-344. D. L. Pyle (ed.), Separations for biotechnology 2. Elsevier, London.
11. Franco, T. T., Andrews, A. T., Asenjo, J. A. 1995. Use of chemically modified proteins to study a single protein property on partitioning in aqueous two-phase systems: Effect of surface hydrophobicity. Biotechnol. Bioeng. 49: 300-308.
12. Franco, T. T., Andrews, A. T., Asenjo, J. A. 1995. Use of chemically modified proteins to study a single protein property on partitioning in aqueous two-phase systems: Effect of surface charge. Biotechnol. Bioeng 49: 309-315.
13. Habeeb, A. F. S. A. 1966. Determination of free amino groups in proteins by trinitrobenzenesulfonic acid. Anal. Biochem. 14: 328-336.
14. Haff L. A., Fagerstam, L. G. 1983. Use of electrophoretic titration curves for predicting optimal chromatographic conditions for fast exchange chromatography of proteins. J. Chromatogr. 266: 409-425.
15. Higginbotham, J. D. 1983. pp. 119-155. in: T. H. Grenby, K. J. Parker, and M. G. Lindley (eds.), Development in sweeteners. Applied Science, London.
16. Klapper, M. H., Klotz, I. M. 1972. pp. 531-536. Acylation with dicarboxylic anhydrides. In: C. H. Hirs and S. N. Timasheff (eds.). Methods in enzymology, Enzyme structure. Academic Press, New York.
17. Kohler, K., Veide, A., Enfors, S.-O. 1991. Partitioning of β-galactosidase fusion proteins in PEG/phosphate aqueous two-phase systems. Enz. Microb. Technol. 13: 204-209.
18. Lamarca, C., Lenhoff, A. M., Dhurjati, P. 1990. Partitioning of host and recombinant cells in aqueous two-phase polymer systems. Biotechnol. Bioeng. 36: 484-492.
19. McKenzie, H. A. 1971. Milk proteins. Chemistry and molecular biology, vol. 2. Academic Press, New York.
20. Miller, S., Janin, J., Lesk, A. M., Chotia, C. 1987. Interior and surface of monomeric proteins. J. Mol. Biol. 196: 641.
21. Okajima, T. Kawata, Y., Hamahuchi, K. 1990. Chemical modification of tryptophan residues. Biochemistry 29: 9168-9175.
22. Pharmacia. 1985. PhastSystem™ user's manual.
23. Rapoport, G., Davis, L., Horecker, B. L. 1969. The subunit structure of the fructose diphosphate aldolase from spinach leaves. Arch. Biochem. Biophys. 132: 286.
24. Riordan, J. F., Vallee, B. L. 1972. Acetylation, pp. 494-499. In: C. H Hirs and S. N. Timasheff (eds.). Methods in enzymology. Enzyme structure. Academic Press, New York.
25. Schmid, F. X. 1990. Spectral methods of characterizing protein conformation and conformational changes. In: T. E. Creighton (ed.), Protein structure. A practical approach. IRL Press, Oxford.
26. Tanford, C. 1973. The hydrophobic effect: Formation of micelles and biological membranes. Wiley, New York.
27. Vithayathil, P., Richards, F. M. 1960. Modification of the amino groups of the peptide component of subtilisin-modified ribonuclease. J. Biol. Chem. 235: 1029.