Bovine myeloperoxidase and lactoperoxidase each contain a high affinity site for calcium

Karla S. Booth; Shioko Kimura; H. Caroline Lee; Masao Ikeda-Saito; Winslow S. Caughey

doi:10.1016/0006-291X(89)92519-9

Bovine myeloperoxidase and lactoperoxidase each contain a high affinity site for calcium

Karla S. Booth, Shioko Kimura, H. Caroline Lee, Masao Ikeda-Saito, Winslow S. Caughey

Institute of Multidisciplinary Research for Advanced Materials (IMRAM)

Research output: Contribution to journal › Article

28 Citations (Scopus)

Abstract

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.

Original language	English
Pages (from-to)	897-902
Number of pages	6
Journal	Biochemical and biophysical research communications
Volume	160
Issue number	2
DOIs	https://doi.org/10.1016/0006-291X(89)92519-9
Publication status	Published - 1989 Apr 28

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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abstract = "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.",

author = "Booth, {Karla S.} and Shioko Kimura and Lee, {H. Caroline} and Masao Ikeda-Saito and Caughey, {Winslow S.}",

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AU - Booth, Karla S.

AU - Kimura, Shioko

AU - Lee, H. Caroline

AU - Ikeda-Saito, Masao

AU - Caughey, Winslow S.

PY - 1989/4/28

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N2 - 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.

AB - 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.

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