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Biochemistry|October 11, 1994
Cysteine 148 in the lactose permease of Escherichia coli is a component of a substrate binding site. 1. Site-directed mutagenesis studiesH Jung, K Jung, H R KabackBiochemistry|April 5, 1994
Dynamics of lactose permease of Escherichia coli determined by site-directed fluorescence labelingK Jung, H Jung, H R KabackProtein Science : a Publication of the Protein Society|July 1, 1994
A conformational change in the lactose permease of Escherichia coli is induced by ligand binding or membrane potentialH Jung, K Jung, H R KabackBiomedica Biochimica Acta|January 1, 1984
Characterization of particulate and soluble variants of the brush-border enzymes alanine aminopeptidase, alkaline phosphatase and gamma-glutamyltransferase in human urineK Jung, M Pergande, U W WischkeAdvances in Biochemical Engineering/Biotechnology|January 1, 1993
Synthesis of L-carnitine by microorganisms and isolated enzymesH Jung, K Jung, H P KleberJournal of Basic Microbiology|January 1, 1987
Regulation of L-carnitine metabolism in Escherichia coliK Jung, H Jung, H P KleberJournal of Basic Microbiology|January 1, 1990
L-carnitine metabolization and osmotic stress response in Escherichia coliH Jung, K Jung, H P KleberPsychotherapie, Psychosomatik, Medizinische Psychologie|March 1, 1992
[Therapeutic factors in psychoanalytic-interactional and depth psychology founded group therapy: an empirical study]S Davies-Osterkamp, K Jung, J OttEnzyme|January 1, 1984
Long-term stability of enzymes in human serum stored in liquid nitrogenK Jung, K Bader, K D GrützmannJournal of Basic Microbiology|January 1, 1990
L-carnitine uptake by Escherichia coliH Jung, K Jung, H P KleberPageof 123