Bovine myeloperoxidase and lactoperoxidase each contain a high affinity site for calcium.
Both bovine myeloperoxidase and lactoperoxidase contain one calcium per iron with no other metal present in significant amount. Calcium is bound with high affinity and is removed upon exposure to 6 M guanidine hydrochloride/EGTA which results in precipitation of protein. Computer amino acid sequence analyses of human myeloperoxidase reveal two plausible calcium binding sites. This is the first evidence for the presence of calcium in these peroxidases.
Booth
K S
KS
Department of Biochemistry, Colorado State University, Fort Collins 80523.
Kimura
S
S
Lee
H C
HC
Ikeda-Saito
M
M
Caughey
W S
WS
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002118:Calcium / Q000378:metabolism*; D002135:Calcium-Binding Proteins / Q000378:metabolism*; D002417:Cattle; D006801:Humans; D007501:Iron / Q000378:metabolism; D007784:Lactoperoxidase / Q000378:metabolism*; D008969:Molecular Sequence Data; D009195:Peroxidase / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D010544:Peroxidases / Q000378:metabolism*; D051381:Rats; D012689:Sequence Homology, Nucleic Acid; D013054:Spectrophotometry, Atomic; D013329:Structure-Activity Relationship
D002135:Calcium-Binding Proteins; D007501:Iron; D007784:Lactoperoxidase; D010544:Peroxidases; D009195:Peroxidase; D002118:Calcium