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FEBS Letters
|
December 15, 1976
Covalent structure of the glycoprotein horseradish peroxidase (EC 1.11.1.7)
K G Welinder
European Journal of Biochemistry
|
September 16, 1985
Plant peroxidases. Their primary, secondary and tertiary structures, and relation to cytochrome c peroxidase
K G Welinder
Analytical Biochemistry
|
October 1, 1988
Generation of peptides suitable for sequence analysis by proteolytic cleavage in reversed-phase high-performance liquid chromatography solvents
K G Welinder
European Journal of Biochemistry
|
June 1, 1979
Amino acid sequence studies of horseradish peroxidase. Amino and carboxyl termini, cyanogen bromide and tryptic fragments, the complete sequence, and some structural characteristics of horseradish peroxidase C
K G Welinder
Biochimica Et Biophysica Acta
|
November 15, 1991
Bacterial catalase-peroxidases are gene duplicated members of the plant peroxidase superfamily
K G Welinder
FEBS Letters
|
July 4, 1983
The oxygen binding site of cytochrome oxidase. Structural predictions on subunit I from amino acid sequences
K G Welinder, L Mikkelsen
FEBS Letters
|
June 23, 1986
Amino acid sequence analysis of the glycopeptides from human complement component C3
K G Welinder, A Svendsen
European Journal of Biochemistry
|
July 1, 1980
Covalent structure of turnip peroxidase 7. Tryptic peptides
G Mazza, K G Welinder
European Journal of Biochemistry
|
July 1, 1980
Covalent structure of turnip peroxidase 7. Cyanogen bromide fragments, complete structure and comparison to horseradish peroxidase C
G Mazza, K G Welinder
European Journal of Biochemistry
|
September 15, 1975
Similarities and differences of five peroxidases from turnip and horseradish. Peptide mapping studies on glycoproteins
K G Welinder, G Mazza
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Search research articles
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Showing results (1-10 of 72) with videos related to
Sort By:
Page
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FEBS Letters
|
December 15, 1976
Covalent structure of the glycoprotein horseradish peroxidase (EC 1.11.1.7)
K G Welinder
European Journal of Biochemistry
|
September 16, 1985
Plant peroxidases. Their primary, secondary and tertiary structures, and relation to cytochrome c peroxidase
K G Welinder
Analytical Biochemistry
|
October 1, 1988
Generation of peptides suitable for sequence analysis by proteolytic cleavage in reversed-phase high-performance liquid chromatography solvents
K G Welinder
European Journal of Biochemistry
|
June 1, 1979
Amino acid sequence studies of horseradish peroxidase. Amino and carboxyl termini, cyanogen bromide and tryptic fragments, the complete sequence, and some structural characteristics of horseradish peroxidase C
K G Welinder
Biochimica Et Biophysica Acta
|
November 15, 1991
Bacterial catalase-peroxidases are gene duplicated members of the plant peroxidase superfamily
K G Welinder
FEBS Letters
|
July 4, 1983
The oxygen binding site of cytochrome oxidase. Structural predictions on subunit I from amino acid sequences
K G Welinder, L Mikkelsen
FEBS Letters
|
June 23, 1986
Amino acid sequence analysis of the glycopeptides from human complement component C3
K G Welinder, A Svendsen
European Journal of Biochemistry
|
July 1, 1980
Covalent structure of turnip peroxidase 7. Tryptic peptides
G Mazza, K G Welinder
European Journal of Biochemistry
|
July 1, 1980
Covalent structure of turnip peroxidase 7. Cyanogen bromide fragments, complete structure and comparison to horseradish peroxidase C
G Mazza, K G Welinder
European Journal of Biochemistry
|
September 15, 1975
Similarities and differences of five peroxidases from turnip and horseradish. Peptide mapping studies on glycoproteins
K G Welinder, G Mazza
Page
of 8