Abstract
Recently it has been reported by Huber et al. [1, 2] that there are no significant structural changes of the backbone atoms in the complex formation of chymotrypsin and pancreatic trypsin inhibitor. Only slight structural re-arrangements of one or a few residues could be observed under X-ray crystal structure analysis.
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Blow, D.M., Wright, C.S., Kukla, D., Rählmann, A., Steigemann, W., Huber, R.: J. molec. Biol. 69, 137–144 (1972).
Rählmann, A., Kukla, D., Schwager, P., Bartels, K., Huber, R.: J. molec. Biol. 77, 417–436 (1973).
Jirgensons, B.: Optical Activity of Proteins and Other Macromolecules. Berlin-Heidelberg-New York: Springer 1973.
Vogel, R. Trautschold, I., Werle, E.: In: Natural Proteinase Inhibitors, pp.89–91: Table XV (citation of TRAUTSCHOLD I., Habilitationsschrift der Med. Fakultät München 1965). New York-London: Academic Press 1968.
Beychok, S.: In: FASMAN, G.D. (Ed.): Poly-α-Amino Acids, pp.293–337. New York: M. Dekker Inc. 1967.
Holzwarth, G., Doty, P.: J. Amer. chem. Soc. 87, 218–228 (1965).
Sarkar, P.K., Doty, P.: Proc. nat. Acad. Sci. (Wash.) 55, 981–989 (1966).
Rosenkranz, H., Scholtan, W.: Z. physiol. Chem. 352, 896–904 (1971). — ROSENKRANZ, H.: Z. Klin. Chem. Klin. Biochem. in press (1974).
Lazdunski, M., Delaage, M.: Biochim. biophys. Acta(Amst.) 140, 417–434 (1967).
Pantaloni, D., D’albis, A., Dessen, P.: J. chim. Phys. 65, 196–205 (1968).
Fric, J., Meloun, B., Sorm, F.: Coll. Czech. Chem. Commun. 36, 2012–2021 (1971).
Vincent, J.P., Chicheportiche, R., Lazdunski, M.: Europ. J. Biochem. 23, 401–411 (1971).
Huber, R., Kukla, D., Rühlmann, A., Epp, O., Formanek, H.: Naturwissenschaften 57, 389–392 (1970).
Scholtan, W., Rosenkranz, H.: Makromol. Chem. 99, 254–274 (1966).
Gabriel, M., Larcher, D., Rinnert, H., Thirion, C., Grange, J.: C.R. Acad. Sci. (Paris) 276, Ser.B 39–41 (1973).
Beychok, S.: Proc. nat. Acad. Sci. (Wash.) 53, 999–1006 (1965).
Edelhoch, H., Steiner, R.F.: J. biol. Chem. 240, 2877–2882 (1965).
Steiner, R.F.: Biochemistry 5, 1964–1970 (1966).
Legrand, M., Viennet, R.: Bull. Soc. chim. France 1965, 679–681.
Tiffany, M. L., Krimm, S.: Biopolymers 8, 347 359 (1969).
Timasheff, S.N., Susi, H., Townend, R., Stevens, L., Gorbunoff, M.J., Kumosinski, T.F.: In: Ramachandran, G.N. (Ed.): Conformation of Biopolymers, pp. 173–196. London-New York: Academic Press 1967.
Vincent, J.P., Lazdunski, M.: Biochemistry 11, 2967–2977 (1972).
Pätter, J.: Z. physiol. Chem. 348, 1197–1206 (1967).
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1974 Springer-Verlag
About this paper
Cite this paper
Rosenkranz, H. (1974). A Study on the Interaction of Trasylol with Trypsin and Kallikrein by Circular Dichroism. In: Fritz, H., Tschesche, H., Greene, L.J., Truscheit, E. (eds) Proteinase Inhibitors. Bayer-Symposium, vol 5. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-87966-1_51
Download citation
DOI: https://doi.org/10.1007/978-3-642-87966-1_51
Publisher Name: Springer, Berlin, Heidelberg
Print ISBN: 978-3-642-87968-5
Online ISBN: 978-3-642-87966-1
eBook Packages: Springer Book Archive