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Journal of Photochemistry and Photobiology. B, Biology|August 14, 1992
Structure, function and organization of antenna polypeptides and antenna complexes from the three families of RhodospirillaneaeR A Brunisholz, H ZuberHoppe-Seyler'S Zeitschrift Fur Physiologische Chemie|July 1, 1979
Structure and function of L-lactate dehydrogenases from thermophilic and mesophilic bacteria. I) Isolation and characterization of lactate dehydrogenases from thermophilic and mesophilic bacilliH P Schär, H ZuberThe Quarterly Journal of Nuclear Medicine : Official Publication of the Italian Association of Nuclear Medicine (AIMN) [And] the International Association of Radiopharmacology (IAR)|June 1, 1995
Effective radiation dose to the patient and to the general population from nuclear medicine procedures: variations in the last twenty-year periodS Garancini, L Bianchi, L Conte, et al.European Journal of Clinical Pharmacology|January 1, 1993
Flumazenil kinetics in the elderlyG Roncari, U Timm, M Zell, et al.Health Physics|September 1, 1991
Too little concern for breast cancer risk in radiation protection estimates?G Schüler, E StollThe International Journal of Biological Markers|January 1, 1997
Tissue polypeptide-specific antigen (TPS) immunoassay in the diagnosis and clinical staging of prostatic carcinoma. Comparison with prostate-specific antigen (PSA)L Ceriani, L Giovanella, M Salvadore, et al.Hoppe-Seyler'S Zeitschrift Fur Physiologische Chemie|June 1, 1983
The complete amino-acid sequence of both subunits of phycoerythrocyanin from the thermophilic cyanobacterium Mastigocladus laminosusP Füglistaller, F Suter, H ZuberBiological Chemistry Hoppe-Seyler|June 1, 1988
The complete amino-acid sequence of the bilin-binding protein from Pieris brassicae and its similarity to a family of serum transport proteins like the retinol-binding proteinsF Suter, H Kayser, H ZuberBiological Chemistry Hoppe-Seyler|September 1, 1987
Structure and function of L-lactate dehydrogenases from thermophilic and mesophilic bacteria, VI. Nucleotide sequences of lactate dehydrogenase genes from the thermophilic bacteria Bacillus stearothermophilus, B. caldolyticus and B. caldotenaxF Zülli, H Weber, H ZuberHoppe-Seyler'S Zeitschrift Fur Physiologische Chemie|July 1, 1983
Structure and function of L-lactate dehydrogenases from thermophilic and mesophilic bacteria. III) The primary structure of thermophilic lactate dehydrogenase from Bacillus stearothermophilus. Hydroxylamine-, o-iodosobenzoic acid- and tryptic-fragments. The complete amino-acid sequenceB Wirz, F Suter, H ZuberPageof 20