Isolation and partial characterization of the formyl peptide receptor components on human neutrophils
The receptor for formylated peptides such as FMLP has been reported to consist of glycoprotein components ranging from 24-95 kDa, and to exhibit both high and low affinity for ligand. Controversy exists on the molecular size and number of these components, and whether the different affinities repres...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
1991 |
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| Reproduktion: |
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 |
|---|---|
| Übergeordnetes Werk: |
in: Biochemical and Biophysical Research Communications - Amsterdam : Elsevier, 174(1991), 1, Seite 84-89 |
| Übergeordnetes Werk: |
volume:174 ; year:1991 ; number:1 ; pages:84-89 |
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| 520 | |a The receptor for formylated peptides such as FMLP has been reported to consist of glycoprotein components ranging from 24-95 kDa, and to exhibit both high and low affinity for ligand. Controversy exists on the molecular size and number of these components, and whether the different affinities represent distinct ligand binding sites. In this study, the receptor was found to be comprised of components, of 94, 68, and ~40 kDa molecular size. Competitive binding inhibition experiments showed that FMLP bound to the components in the following order from highest to lowest affinity: 68 kDa > ~40 kDa > 94 kDa. Our findings suggest that the FMLP receptor of human neutrophils contains at least three components, and that each component has a different affinity for FMLP. | ||
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(DE-627)NLEJ183540700 (DE-599)GBVNLZ183540700 DE-627 ger DE-627 rakwb eng Isolation and partial characterization of the formyl peptide receptor components on human neutrophils 1991 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The receptor for formylated peptides such as FMLP has been reported to consist of glycoprotein components ranging from 24-95 kDa, and to exhibit both high and low affinity for ligand. Controversy exists on the molecular size and number of these components, and whether the different affinities represent distinct ligand binding sites. In this study, the receptor was found to be comprised of components, of 94, 68, and ~40 kDa molecular size. Competitive binding inhibition experiments showed that FMLP bound to the components in the following order from highest to lowest affinity: 68 kDa > ~40 kDa > 94 kDa. Our findings suggest that the FMLP receptor of human neutrophils contains at least three components, and that each component has a different affinity for FMLP. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 De Nardin, E. oth Radel, S.J. oth Genco, R.J. oth in Biochemical and Biophysical Research Communications Amsterdam : Elsevier 174(1991), 1, Seite 84-89 (DE-627)NLEJ176855645 (DE-600)1461396-7 0006-291X nnns volume:174 year:1991 number:1 pages:84-89 http://dx.doi.org/10.1016/0006-291X(91)90488-S GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 174 1991 1 84-89 |
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(DE-627)NLEJ183540700 (DE-599)GBVNLZ183540700 DE-627 ger DE-627 rakwb eng Isolation and partial characterization of the formyl peptide receptor components on human neutrophils 1991 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The receptor for formylated peptides such as FMLP has been reported to consist of glycoprotein components ranging from 24-95 kDa, and to exhibit both high and low affinity for ligand. Controversy exists on the molecular size and number of these components, and whether the different affinities represent distinct ligand binding sites. In this study, the receptor was found to be comprised of components, of 94, 68, and ~40 kDa molecular size. Competitive binding inhibition experiments showed that FMLP bound to the components in the following order from highest to lowest affinity: 68 kDa > ~40 kDa > 94 kDa. Our findings suggest that the FMLP receptor of human neutrophils contains at least three components, and that each component has a different affinity for FMLP. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 De Nardin, E. oth Radel, S.J. oth Genco, R.J. oth in Biochemical and Biophysical Research Communications Amsterdam : Elsevier 174(1991), 1, Seite 84-89 (DE-627)NLEJ176855645 (DE-600)1461396-7 0006-291X nnns volume:174 year:1991 number:1 pages:84-89 http://dx.doi.org/10.1016/0006-291X(91)90488-S GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 174 1991 1 84-89 |
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(DE-627)NLEJ183540700 (DE-599)GBVNLZ183540700 DE-627 ger DE-627 rakwb eng Isolation and partial characterization of the formyl peptide receptor components on human neutrophils 1991 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The receptor for formylated peptides such as FMLP has been reported to consist of glycoprotein components ranging from 24-95 kDa, and to exhibit both high and low affinity for ligand. Controversy exists on the molecular size and number of these components, and whether the different affinities represent distinct ligand binding sites. In this study, the receptor was found to be comprised of components, of 94, 68, and ~40 kDa molecular size. Competitive binding inhibition experiments showed that FMLP bound to the components in the following order from highest to lowest affinity: 68 kDa > ~40 kDa > 94 kDa. Our findings suggest that the FMLP receptor of human neutrophils contains at least three components, and that each component has a different affinity for FMLP. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 De Nardin, E. oth Radel, S.J. oth Genco, R.J. oth in Biochemical and Biophysical Research Communications Amsterdam : Elsevier 174(1991), 1, Seite 84-89 (DE-627)NLEJ176855645 (DE-600)1461396-7 0006-291X nnns volume:174 year:1991 number:1 pages:84-89 http://dx.doi.org/10.1016/0006-291X(91)90488-S GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 174 1991 1 84-89 |
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(DE-627)NLEJ183540700 (DE-599)GBVNLZ183540700 DE-627 ger DE-627 rakwb eng Isolation and partial characterization of the formyl peptide receptor components on human neutrophils 1991 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The receptor for formylated peptides such as FMLP has been reported to consist of glycoprotein components ranging from 24-95 kDa, and to exhibit both high and low affinity for ligand. Controversy exists on the molecular size and number of these components, and whether the different affinities represent distinct ligand binding sites. In this study, the receptor was found to be comprised of components, of 94, 68, and ~40 kDa molecular size. Competitive binding inhibition experiments showed that FMLP bound to the components in the following order from highest to lowest affinity: 68 kDa > ~40 kDa > 94 kDa. Our findings suggest that the FMLP receptor of human neutrophils contains at least three components, and that each component has a different affinity for FMLP. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 De Nardin, E. oth Radel, S.J. oth Genco, R.J. oth in Biochemical and Biophysical Research Communications Amsterdam : Elsevier 174(1991), 1, Seite 84-89 (DE-627)NLEJ176855645 (DE-600)1461396-7 0006-291X nnns volume:174 year:1991 number:1 pages:84-89 http://dx.doi.org/10.1016/0006-291X(91)90488-S GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 174 1991 1 84-89 |
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(DE-627)NLEJ183540700 (DE-599)GBVNLZ183540700 DE-627 ger DE-627 rakwb eng Isolation and partial characterization of the formyl peptide receptor components on human neutrophils 1991 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The receptor for formylated peptides such as FMLP has been reported to consist of glycoprotein components ranging from 24-95 kDa, and to exhibit both high and low affinity for ligand. Controversy exists on the molecular size and number of these components, and whether the different affinities represent distinct ligand binding sites. In this study, the receptor was found to be comprised of components, of 94, 68, and ~40 kDa molecular size. Competitive binding inhibition experiments showed that FMLP bound to the components in the following order from highest to lowest affinity: 68 kDa > ~40 kDa > 94 kDa. Our findings suggest that the FMLP receptor of human neutrophils contains at least three components, and that each component has a different affinity for FMLP. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 De Nardin, E. oth Radel, S.J. oth Genco, R.J. oth in Biochemical and Biophysical Research Communications Amsterdam : Elsevier 174(1991), 1, Seite 84-89 (DE-627)NLEJ176855645 (DE-600)1461396-7 0006-291X nnns volume:174 year:1991 number:1 pages:84-89 http://dx.doi.org/10.1016/0006-291X(91)90488-S GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 174 1991 1 84-89 |
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isolation and partial characterization of the formyl peptide receptor components on human neutrophils |
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Isolation and partial characterization of the formyl peptide receptor components on human neutrophils |
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The receptor for formylated peptides such as FMLP has been reported to consist of glycoprotein components ranging from 24-95 kDa, and to exhibit both high and low affinity for ligand. Controversy exists on the molecular size and number of these components, and whether the different affinities represent distinct ligand binding sites. In this study, the receptor was found to be comprised of components, of 94, 68, and ~40 kDa molecular size. Competitive binding inhibition experiments showed that FMLP bound to the components in the following order from highest to lowest affinity: 68 kDa > ~40 kDa > 94 kDa. Our findings suggest that the FMLP receptor of human neutrophils contains at least three components, and that each component has a different affinity for FMLP. |
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The receptor for formylated peptides such as FMLP has been reported to consist of glycoprotein components ranging from 24-95 kDa, and to exhibit both high and low affinity for ligand. Controversy exists on the molecular size and number of these components, and whether the different affinities represent distinct ligand binding sites. In this study, the receptor was found to be comprised of components, of 94, 68, and ~40 kDa molecular size. Competitive binding inhibition experiments showed that FMLP bound to the components in the following order from highest to lowest affinity: 68 kDa > ~40 kDa > 94 kDa. Our findings suggest that the FMLP receptor of human neutrophils contains at least three components, and that each component has a different affinity for FMLP. |
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The receptor for formylated peptides such as FMLP has been reported to consist of glycoprotein components ranging from 24-95 kDa, and to exhibit both high and low affinity for ligand. Controversy exists on the molecular size and number of these components, and whether the different affinities represent distinct ligand binding sites. In this study, the receptor was found to be comprised of components, of 94, 68, and ~40 kDa molecular size. Competitive binding inhibition experiments showed that FMLP bound to the components in the following order from highest to lowest affinity: 68 kDa > ~40 kDa > 94 kDa. Our findings suggest that the FMLP receptor of human neutrophils contains at least three components, and that each component has a different affinity for FMLP. |
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