Abstract
A very versatile chemical method for immobilizing enzymes and other proteins is intermolecular cross-linking with multifunctional reagents. The method can produce enzyme conjugates of diverse physical character depending on the conditions employed. Thus, conjugates can be prepared that are water-soluble or water-insoluble; granular, gel-like, or filamentous in nature; or that are pure protein. It is reliable and inexpensive.
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References
Broun, G., Selegny, E., Avrameas, S., and Thomas, D., 1969, Enzymatically active membranes: some properties of cellophane membranes supporting cross-linked enzymes, Biochim. Biophys. Acta 185: 258.
Broun, G., Selegny, E., Minh, C. T., and Thomas, D., 1970, Facilitated transport of CO2 across a membrane bearing carbonic anhydrase, FEBS Letters 7: 223.
Broun, G., Thomas, D., Gellf, G., Domurado, D., Berjonneau, A. M., and Guillon, C., 1973, New methods for binding enzyme molecules into a water-insoluble matrix: properties after insolubilization, Biotechnol. Bioeng. 15: 359.
Chang, T. M. S., 1971, Stabilization of enzymes by microencapsulation with a concentrated protein solution or by microencapsulation followed by cross-linking with glutaraldehyde, Biochem. Biophys. Res. Commun. 44: 1531.
Fasold, H., Klappenberger, J., Meyer, C., and Remold, H., 1971, Bifunctional reagents for the cross-linking of proteins, Angew. Chem. Int. Ed. Engl. 10: 795.
Ferrier, L. K., Richardson, T., and Olson, N. F., 1972, Crystalline catalase insolubilized with glutaraldehyde, Enzyynwlogia 42: 273.
Glassmeyer, C. K., and Ogle, J. D., 1971, Properties of an insoluble form of trypsin, Biochemistry 10: 786.
Goldman, R., and Katchalski, E., 1971, Kinetic behavior of a two-enzyme membrane carrying out a consecutive set of reactions, J. Theoret. Biol. 32: 243.
Goldman, R., Kedem, O., Silman, I. H., Caplan, S. R., and Katchalski, E., 1968, Papain-collodion membranes: I. Preparation and properties, Biochemistry 7: 486.
Habeeb, A. F. S. A., 1967, Preparation of enzymically active, water-insoluble derivatives of trypsin, Arch. Biochem. Biophys. 119: 264.
Haynes, R., and Walsh, K. A., 1969, Enzyme envelopes on colloidal particles, Biochem. Biophys. Res. Commun. 36: 235.
Inman, J. K., and Dintzis, H. M., 1969, The derivatization of cross-linked polyacrylamide beads: controlled introduction of functional groups for the preparation of special-purpose, biochemical adsorbents, Biochemistry 8: 4074.
Jansen, E. F., and Olson, A. C., 1969, Properties and enzymatic activities of papain insolubilized with glutaraldehyde, Arch. Biochem Biophys. 129: 221.
Jansen, E. F., Tomimatsu, Y., and Olson, A. C., 1971, Cross-linking of a-chymotrypsin and other proteins by reaction with glutaraldehyde, Arch. Biochem. Biophys. 144: 394.
Jaworek, D., 1974, New immobilization techniques and supports, in: Enzyme Engineering, Vol. 2 (E. K. Pye and L. B. Wingard, Jr., eds.), pp. 105–114, Plenum Press, New York.
Ogata, K., Ottesen, M., and Svendsen, I., 1968, Preparation of water-insoluble, enzymatically active derivatives of subtilisin type Nova by cross-linking with glutaraldehyde, Biochim. Biophys. Acta 159: 403.
Ottesen, M., and Svensson, B., 1971, Modification of papain by treatment with glutaraldehyde under reducing and non-reducing conditions, Compt. Rend. Tray. Lab. Carlsberg 38: 171.
Patel, R. P., and Price, S., 1967, Derivatives of proteins. I Polymerization of a-chymotrypsin by use of N-ethyl-5-phenylisoxazolium-3’-sulfonate, Biopolymers 5: 583.
Patramani, I., Katsiri, K., Pistevou, E., Kalogerakos, T., Pavlatos, M., and Evangelopoulos, A. E., 1969, Glutamic-aspartic transaminase-antitransaminase interaction: a method for antienzyme purification, Eur. J. Biochem. 11: 28.
Quiocho, F. A., and Richards, F. M., 1964, Intermolecular cross-linking of a protein in the crystalline state: carboxypeptidase A, Proc. Natl. Acad. Sci. U.S. 52: 833.
Rao, S. S., Patki, V. M., and Kulkarni, A. D., 1970, Preparation of active insoluble pepsin, Indian J. Biochem. 7: 210.
Ruoho, A., Bartlett, P. A., Dutton, A., and Singer, S.J., 1975, A disulfide-bridge bifunctional imidoester as a reversible cross-linking reagent, Biochem. Biophys. Res. Commun. 63: 417.
Schejter, A., and Bar-Eli, A., 1970, Preparation and properties of cross-linked water-insoluble catalase, Arch. Biochem. Biophys. 136: 325.
Selegny, E., Broun, G., and Thomas, D., 1971, Enzymatically active model-membranes: experimental illustrations and calculations on the basis of diffusion reaction kinetics of their functioning, of regulatory effects, of facilitated, retarded and active transports, Physiol. Vegetale 9: 25.
Silman, I. H., Albu-Weisenberg, M., and Katchalski, E., 1966, Some water-insoluble papain derivatives, Biopolymers 4: 441.
Tomimatsu, Y., Jansen, E. F., Gaffield, and Olson, A. C., 1971, Physical chemical observations on the achymotrypsin glutaraldehyde system during formation of an insoluble derivative, J. Colloid Interface Sci. 36: 51.
Walsh, K. A., Houston, L. L., and Kenner, R. A., 1970, Chemical modification of bovine trypsinogen and trypsin, in: Structure—Function Relationships of Proteolytic Enzymes ( P. Desnuelle, H. Neurath, and M. Ottesen, eds.), pp. 56–69, Academic Press, Inc., New York.
Wetz, K., Fasold, H., and Meyer, C., 1974, Synthesis of “long,” hydrophilic, protein cross-linking reagents, Anal. Biochem. 58: 347.
Wold, F., 1972, Bifunctional reagents, in: Methods in Enzymology, Vol. 25B ( C. H. W. Hirs and S. N. Timasheff, eds.), pp. 623–651, Academic Press, Inc., New York.
Zaborsky, O. R., 1973, Immobilized Enzymes, CRC Press, Cleveland, Ohio.
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© 1977 Plenum Press, New York
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Zaborsky, O.R. (1977). Covalent Linkage: III. Immobilization of Enzymes by Intermolecular Cross-Linking. In: Chang, T.M.S. (eds) Biomedical Applications of Immobilized Enzymes and Proteins. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-2610-6_4
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DOI: https://doi.org/10.1007/978-1-4684-2610-6_4
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