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H Fasold

Showing results (21-30 of 75) with videos related to

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FEBS Letters|November 15, 1974
The use of a new series of cleavable protein-crosslinkers on the Escherichia coli ribosomeL C Lutter, F Ortanderl, H Fasold
European Journal of Biochemistry|July 3, 1978
The synthesis of a photoreactive puromycin analogue and its application for labeling proteins in the 50-S subunit of Escherichia coli ribosomesF Krassnigg, V A Erdmann, H Fasold
Biochimica Et Biophysica Acta|April 14, 1989
Bile acid binding proteins in hepatocellular membranes of newborn and adult rats. Identification of transport proteins with azidobenzamidotauro[14C]cholate ([14C]ABATC)K Ziegler, M Frimmer, S Müllner, et al.
Naunyn-Schmiedeberg'S Archives of Pharmacology|June 1, 1982
Affinity labels for membrane components involved in the uptake of bile acids and of phallotoxins by hepatocytes. Development of covalently binding derivatives of bile acids and of compounds related to cholecystographic agentsK Ziegler, M Frimmer, W Möller, et al.
FEBS Letters|August 1, 1978
Isolation of native microtubules from porcine brain and characterization of SH groups essential for polymerization at the GTP binding sitesK Mann, M Giesel, H Fasold, et al.
Angewandte Chemie (International Ed. in English)|November 1, 1971
Bifunctional reagents for the crosslinking of proteinsH Fasold, J Klappenberger, C Meyer, et al.
Biochimica Et Biophysica Acta|June 13, 1984
3'-Isothiocyanatobenzamido[3H]cholate, a new affinity label for hepatocellular membrane proteins responsible for the uptake of both bile acids and phalloidinK Ziegler, M Frimmer, S Müllner, et al.
Analytical Biochemistry|November 1, 1980
Reagents suitable for the crosslinking of nucleic acids to proteinsG Fink, H Fasold, W Rommel, et al.
The Journal of Membrane Biology|October 20, 1976
A study of the relationship between inhibition of anion exchange and binding to the red blood cell membrane of 4,4'-diisothiocyano stilbene-2,2'-disulfonic acid (DIDS) and its dihydro derivative (H2DIDS)S Lepke, H Fasold, M Pring, et al.
Journal of Cellular Physiology|December 1, 1975
Chemical modification of membrane proteins in relation to inhibition of anion exchange in human red blood cellsL Zaki, H Fasold, B Schuhmann, et al.
Pageof 8

Showing results (21-30 of 75) with videos related to

Sort By:
Pageof 8
FEBS Letters|November 15, 1974
The use of a new series of cleavable protein-crosslinkers on the Escherichia coli ribosomeL C Lutter, F Ortanderl, H Fasold
European Journal of Biochemistry|July 3, 1978
The synthesis of a photoreactive puromycin analogue and its application for labeling proteins in the 50-S subunit of Escherichia coli ribosomesF Krassnigg, V A Erdmann, H Fasold
Biochimica Et Biophysica Acta|April 14, 1989
Bile acid binding proteins in hepatocellular membranes of newborn and adult rats. Identification of transport proteins with azidobenzamidotauro[14C]cholate ([14C]ABATC)K Ziegler, M Frimmer, S Müllner, et al.
Naunyn-Schmiedeberg'S Archives of Pharmacology|June 1, 1982
Affinity labels for membrane components involved in the uptake of bile acids and of phallotoxins by hepatocytes. Development of covalently binding derivatives of bile acids and of compounds related to cholecystographic agentsK Ziegler, M Frimmer, W Möller, et al.
FEBS Letters|August 1, 1978
Isolation of native microtubules from porcine brain and characterization of SH groups essential for polymerization at the GTP binding sitesK Mann, M Giesel, H Fasold, et al.
Angewandte Chemie (International Ed. in English)|November 1, 1971
Bifunctional reagents for the crosslinking of proteinsH Fasold, J Klappenberger, C Meyer, et al.
Biochimica Et Biophysica Acta|June 13, 1984
3'-Isothiocyanatobenzamido[3H]cholate, a new affinity label for hepatocellular membrane proteins responsible for the uptake of both bile acids and phalloidinK Ziegler, M Frimmer, S Müllner, et al.
Analytical Biochemistry|November 1, 1980
Reagents suitable for the crosslinking of nucleic acids to proteinsG Fink, H Fasold, W Rommel, et al.
The Journal of Membrane Biology|October 20, 1976
A study of the relationship between inhibition of anion exchange and binding to the red blood cell membrane of 4,4'-diisothiocyano stilbene-2,2'-disulfonic acid (DIDS) and its dihydro derivative (H2DIDS)S Lepke, H Fasold, M Pring, et al.
Journal of Cellular Physiology|December 1, 1975
Chemical modification of membrane proteins in relation to inhibition of anion exchange in human red blood cellsL Zaki, H Fasold, B Schuhmann, et al.
Pageof 8