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FEBS Letters|June 23, 1986
Amino acid sequence analysis of the glycopeptides from human complement component C3K G Welinder, A SvendsenEuropean Journal of Biochemistry|September 16, 1985
Plant peroxidases. Their primary, secondary and tertiary structures, and relation to cytochrome c peroxidaseK G WelinderAnalytical Biochemistry|October 1, 1988
Generation of peptides suitable for sequence analysis by proteolytic cleavage in reversed-phase high-performance liquid chromatography solventsK G WelinderEuropean 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 CK G WelinderBiochimica Et Biophysica Acta|November 15, 1991
Bacterial catalase-peroxidases are gene duplicated members of the plant peroxidase superfamilyK G WelinderFEBS Letters|July 4, 1983
The oxygen binding site of cytochrome oxidase. Structural predictions on subunit I from amino acid sequencesK G Welinder, L MikkelsenEuropean Journal of Biochemistry|July 1, 1980
Covalent structure of turnip peroxidase 7. Tryptic peptidesG Mazza, K G WelinderEuropean Journal of Biochemistry|July 1, 1980
Covalent structure of turnip peroxidase 7. Cyanogen bromide fragments, complete structure and comparison to horseradish peroxidase CG Mazza, K G WelinderEuropean Journal of Biochemistry|September 15, 1975
Similarities and differences of five peroxidases from turnip and horseradish. Peptide mapping studies on glycoproteinsK G Welinder, G MazzaEuropean Journal of Biochemistry|March 1, 1977
Amino-acid sequences of heme-linked, histidine-containing peptides of five peroxidases from horseradish and turnipK G Welinder, G MazzaPageof 17