Sökning: L773:0022 1767
> (1985-1989) >
Ig-binding bacteria...
Ig-binding bacterial proteins also bind proteinase inhibitors
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- Sjöbring, U (författare)
- Lund University,Lunds universitet,Avdelningen för mikrobiologi, immunologi och glykobiologi - MIG,Institutionen för laboratoriemedicin,Medicinska fakulteten,Division of Microbiology, Immunology and Glycobiology - MIG,Department of Laboratory Medicine,Faculty of Medicine
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Trojnar, J (författare)
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- Grubb, A (författare)
- Lund University,Lunds universitet,Medicinska fakulteten,Cystatin C, njursjukdom, amyloidos och antibiotika,Forskargrupper vid Lunds universitet,Faculty of Medicine,Cystatin C, renal disease, amyloidosis and antibiotics,Lund University Research Groups
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- Akerström, B (författare)
- Lund University,Lunds universitet,Infektionsmedicin,Sektion III,Institutionen för kliniska vetenskaper, Lund,Medicinska fakulteten,Antioxidationsmedicin,Forskargrupper vid Lunds universitet,Infection Medicine (BMC),Section III,Department of Clinical Sciences, Lund,Faculty of Medicine,Antioxidation medicine,Lund University Research Groups
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- Björck, L (författare)
- Lund University,Lunds universitet,Infektionsmedicin,Sektion III,Institutionen för kliniska vetenskaper, Lund,Medicinska fakulteten,Molekylär patogenes,Forskargrupper vid Lunds universitet,epIgG,Infection Medicine (BMC),Section III,Department of Clinical Sciences, Lund,Faculty of Medicine,Molecular Pathogenesis,Lund University Research Groups
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(creator_code:org_t)
- 1989
- 1989
- Engelska.
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Ingår i: Journal of immunology. - 0022-1767. ; 143:9, s. 54-2948
- Relaterad länk:
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https://www.jimmunol...
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https://lup.lub.lu.s...
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Abstract
Ämnesord
Stäng
- Protein G is a streptococcal cell wall protein with separate binding sites for IgG and human serum albumin (HSA). In the present work it was demonstrated that alpha 2-macroglobulin (alpha 2M) and kininogen, two proteinase inhibitors of human plasma, bound to protein G, whereas 23 other human proteins showed no affinity. alpha 2M was found to interact with the IgG-binding domains of protein G, and in excess alpha 2M inhibited IgG binding and vice versa. A synthetic peptide, corresponding to one of the homologous IgG-binding domains of protein G, blocked binding of protein G to alpha 2M. Protein G showed affinity for both native and proteinase complexed alpha 2M but did not bind to the reduced form of alpha 2M, or to the C-terminal domain of the protein known to interact with alpha 2M receptors on macrophages. Binding of protein G to alpha 2M and kininogen did not interfere with their inhibitory activity on proteinases, and the interaction between protein G and the two proteinase inhibitors was not due to proteolytic activity of protein G. The finding that protein G has affinity for proteinase inhibitors was generalized to comprise also other Ig binding bacterial proteins. Thus, alpha 2M and kininogen, were shown to bind both protein A of Staphylococcus aureus and protein L of Peptococcus magnus. The results described above suggest that Ig-binding proteins are involved in proteolytic events, which adds a new and perhaps functional aspect to these molecules.
Ämnesord
- MEDICIN OCH HÄLSOVETENSKAP -- Medicinska och farmaceutiska grundvetenskaper -- Immunologi inom det medicinska området (hsv//swe)
- MEDICAL AND HEALTH SCIENCES -- Basic Medicine -- Immunology in the medical area (hsv//eng)
Nyckelord
- Bacterial Proteins/metabolism
- In Vitro Techniques
- Kininogens/metabolism
- Lymphokines/metabolism
- Molecular Weight
- Nerve Tissue Proteins/metabolism
- Prostatic Secretory Proteins
- Protease Inhibitors/metabolism
- Protein Binding
- Streptococcus
- Trypsin/metabolism
- alpha-Macroglobulins/metabolism
Publikations- och innehållstyp
- art (ämneskategori)
- ref (ämneskategori)
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