Martin-Luther-Universität Halle-Wittenberg

Labor BCBT

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1986-1990

1986

Rudolph, R., Fuchs, I. & Jaenicke, R. (1986)
Biochemistry 25, 1662-1669
Reassociation of Dimeric Cytoplasmic Malate Dehydrogenase Is Determined by Slow and Very Slow Folding Reactions.

Jaenicke, R. & Rudolph, R. (1986)
Meth. Enzymol. Vol. 131, 218-250
Refolding and Association of Oligomeric Proteins.

Söylemez, Z., Rudolph, R. & Jaenicke, R. (1986)
Biol. Chem. Hoppe-Seyler 367, 705-713
Isoproterenol Inhibition of Horse Serum Cholinesterase Is Connected with Subunit Dissociation.

Jaenicke, R., Rudolph, R. & Feingold, D.S. (1986)
Biochemistry 25, 7283-7287
Dissociation and in vitro Reconstitution of Bovine Liver Uridine Diphosphoglucose Dehydrogenase. The Paired Subunit Nature of the Enzyme.

1987

Opitz, U., Rudolph, R., Jaenicke, R., Ericsson, L. & Neurath, H. (1987)
Biochemistry 26, 1399-1406
Proteolytic Dimers of Porcine Muscle Lactate Dehydrogenase: Characterization, Folding, and Reconstitution of the Truncated and Nicked Polypeptide Chain.

Teschner, W., Rudolph, R. & Garel, J.-R. (1987)
Biochemistry 26, 2791-2796
Intermediates on the Folding Pathway of Octopine Dehydrogenase from Pecten jacobaeus.

1989

Jaenicke, R. & Rudolph, R. (1989)
Protein Structure, A Practical Approach (Creighton, T.E., ed.) pp 191-223, IRL-Press, Oxford, New York, Tokyo
Folding Proteins

Teschner, W. & Rudolph, R. (1989)
Biochem. J. 260, 583-587
A Carboxypeptidase Y Pulse Method to Study the Accessibility of the C-Terminal End During the Refolding of Ribonuclease A.

Buchner, J. & Rudolph, R. (1989)
Dechema Biotechnology Conferences 3, 1035-1040
Renaturation of Antibodies after Expression in E.coli.

1990

Scheibe, R., Rudolph, R., Reng, W. & Jaenicke, R. (1990)
Eur. J. Biochem. 189, 581-587
Structural and Catalytic Properties of Oxidized and Reduced Chloroplast NADP-Malate Dehydrogenase upon Denaturation and Renaturation.

Rudolph, R., Siebendritt, R., Neßlauer, G., Sharma, A.K. & Jaenicke, R. (1990)
Proc. Natl. Acad. Sci. U.S.A. 87, 4625-4629
Folding of an all-ß Protein: Independent Domain Folding in gamma II-Crystallin from Calf Eye Lens.

Rudolph, R. (1990)
Modern Methods in Protein and Nucleic Acid Research (Tschesche, H., ed.) pp. 149-171, Walter de Gruyter, Berlin, N.Y.,
Renaturation of Recombinant, Disulfide-Bonded Proteins from "Inclusion Bodies".

Sharma, A.K., Minke-Gogl, V., Gohl, P., Siebendritt, R., Jaenicke, R. & Rudolph, R. (1990)
Eur. J. Biochem. 194, 603-609
Limited Proteolysis of  II-Crystallin from Calf Eye Lens: Physicochemical Studies on the N-Terminal Domain and the Intact Two-Domain Protein.

Martin, U., Fischer, S., Kohnert, U., Lill, H., Rudolph, R., Sponer, G., Stern, A. & Strein, K. (1990)
Z. Kardiol. 79, Suppl. 3, 167-170
Properties of a Novel Plasminogen Activator (BM 06.022) Produced in Escherichia coli.

Buchner, J. & Rudolph, R. (1990)
Biotechnology International (North, K., ed.) pp. 91-96, Century Press Ltd., London
Production of a Functional Antibody Fab-Fragment from E.coli Inclusion Bodies: In vitro Renaturation, Purification and Characterization.

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