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Protein L from Pept...
Protein L from Peptostreptococcus magnus binds to the kappa light chain variable domain
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- Nilson, B H (författare)
- Lund University,Lunds universitet,Avdelningen för medicinsk mikrobiologi,Institutionen för laboratoriemedicin,Medicinska fakulteten,Division of Medical Microbiology,Department of Laboratory Medicine,Faculty of Medicine
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- Solomon, A (författare)
- University of Tennessee
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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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- Akerström, B (författare)
- Lund University,Lunds universitet,Infektionsmedicin,Sektion III,Institutionen för kliniska vetenskaper, Lund,Medicinska fakulteten,Infection Medicine (BMC),Section III,Department of Clinical Sciences, Lund,Faculty of Medicine
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(creator_code:org_t)
- 1992
- 1992
- Engelska.
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Ingår i: Journal of Biological Chemistry. - 0021-9258. ; 267:4, s. 9-2234
- Relaterad länk:
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http://www.jbc.org/c...
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Abstract
Ämnesord
Stäng
- Protein L is an immunoglobulin light chain-binding protein expressed by some strains of the anaerobic bacterial species Peptostreptococcus magnus. The major variable region subgroups of human kappa and lambda light chains were tested for protein L binding; V kappa I, V kappa III, and V kappa IV bound protein L, whereas no binding occurred with proteins of the V kappa II subgroup or with any lambda light chain subgroups. Studies of the protein L binding capacity of naturally occurring VL fragments, and VL- and CL-related trypsin- and pepsin-derived peptides prepared from a kappa I light chain, localized the site of interaction to the VL domain. The affinity constant for the binding to an isolated V kappa I fragment was comparable to that for the native protein (Ka 0.9 x 10(9) M-1 and Ka 1.5 x 10(9) M-1, respectively). No binding occurred with CL-related fragments. Extensive reduction and alkylation of the V kappa fragment or the native kappa chain resulted in complete loss of protein L binding. Although it is possible, from comparative amino acid sequence data, to identify certain VL-framework region residues that account for the selective binding of protein L by kappa I, kappa III, and kappa IV proteins, our studies indicate that this interaction is essentially dependent upon the tertiary structural integrity of the kappa chain VL domain.
Ämnesord
- MEDICIN OCH HÄLSOVETENSKAP -- Medicinska och farmaceutiska grundvetenskaper -- Läkemedelskemi (hsv//swe)
- MEDICAL AND HEALTH SCIENCES -- Basic Medicine -- Medicinal Chemistry (hsv//eng)
Nyckelord
- Amino Acid Sequence
- Bacterial Proteins
- Chromatography, Liquid
- Electrophoresis, Polyacrylamide Gel
- Humans
- Immunoglobulin Variable Region
- Immunoglobulin kappa-Chains
- Molecular Sequence Data
- Pepsin A
- Peptostreptococcus
- Protein Conformation
- Radioimmunoassay
- Trypsin
- X-Ray Diffraction
- Journal Article
- Research Support, Non-U.S. Gov't
- Research Support, U.S. Gov't, P.H.S.
Publikations- och innehållstyp
- art (ämneskategori)
- ref (ämneskategori)
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