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Staphylococcal neutral phosphatase
Author(s) -
YOUSIF YEHIA,
SCHILTZ EMILE,
OKADA KANAME,
BATSFORD STEPHEN,
VOGT ARNOLD
Publication year - 1994
Publication title -
apmis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.909
H-Index - 88
eISSN - 1600-0463
pISSN - 0903-4641
DOI - 10.1111/j.1699-0463.1994.tb05250.x
Subject(s) - isoelectric point , polyclonal antibodies , biochemistry , chemistry , antibody , enzyme , microbiology and biotechnology , alkaline phosphatase , staphylococcus aureus , phosphatase , affinity chromatography , acid phosphatase , protein a , ultracentrifuge , biology , bacteria , genetics , immunology
Staphylococcal neutral phosphatase (NPtase) was purified from two Staphylococcus aureus strains by sequential high salt extraction, ultracentrifugation and ion exchange chromatography. The enzyme showed maximum phosphatase activity at neutral pH, appeared as two bands in SDS‐PAGE (31 and 32 kDa), and the isoelectric point was > 10. No close similarity between NPtase and other known bacterial proteins in respect of their N‐terminal amino acid sequences was found. Purified NPtase bound rat and human polyclonal IgG [intact and F(ab') 2 fragments], IgM, IgA, intact myeloma immunoglobulins, myeloma light chains, gamma heavy chain and, with a much lower affinity, Fc fragments. Furthermore, NPtase can bind serum albumin. Heparin, a highly negatively charged molecule, significantly inhibited NPtase binding to immunoglobulins and HSA, but did not inhibit the binding of specific antibodies to NPtase; this indicates that charge interactions are important. The newly characterized staphylococcal phosphatase with binding properties for immunoglobulin is an interesting bacterial protein that could be involved in post‐infectious sequelae.