Vacuum‐UV‐Radiation‐Induced Structural‐Functional Changes in Serum Albumin Molecules
Abstract Using the methods of spectrophotometry, luminescent analysis, and fluorescent probes, we have investigated the structural changes in bull serum albumin (BSA) molecules induced by the action of vacuum UV (VUV) radiation (λ = 131161 nm, dose — 6300 kJ/$ m^{2} $). It has been found that the ch...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Artyukhov, V. G. [verfasserIn] |
|---|
| Format: |
Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2001 |
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| Anmerkung: |
© Plenum Publishing Corporation 2001 |
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| Übergeordnetes Werk: |
Enthalten in: Journal of applied spectroscopy - Kluwer Academic Publishers-Plenum Publishers, 1966, 68(2001), 2 vom: März, Seite 291-298 |
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volume:68 ; year:2001 ; number:2 ; month:03 ; pages:291-298 |
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10.1023/A:1019224404819 |
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| 520 | |a Abstract Using the methods of spectrophotometry, luminescent analysis, and fluorescent probes, we have investigated the structural changes in bull serum albumin (BSA) molecules induced by the action of vacuum UV (VUV) radiation (λ = 131161 nm, dose — 6300 kJ/$ m^{2} $). It has been found that the change in the spectral‐fluorescent properties of BSA molecules after irradiation under the conditions of different microsurroundings is caused by the “unrolling” of the protein globule due to the weakening and rupture of weak intramolecular bonds as well as by the photomodification of the aromatic amino acid residues in the composition of the protein macromolecule. A scheme of the phototransformation processes in the BSA molecules under the action of vacuum ultraviolet has been drawn. In accordance with this scheme the VUV light in the region of absorption of peptide bonds of protein molecules induces a disturbance in their third‐order structure, which leads to a modification of the state of aromatic amino acid residues and a change in the functional properties of protein macromolecules. | ||
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10.1023/A:1019224404819 doi (DE-627)OLC2034664051 (DE-He213)A:1019224404819-p DE-627 ger DE-627 rakwb eng 530 VZ 11 ssgn Artyukhov, V. G. verfasserin aut Vacuum‐UV‐Radiation‐Induced Structural‐Functional Changes in Serum Albumin Molecules 2001 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Plenum Publishing Corporation 2001 Abstract Using the methods of spectrophotometry, luminescent analysis, and fluorescent probes, we have investigated the structural changes in bull serum albumin (BSA) molecules induced by the action of vacuum UV (VUV) radiation (λ = 131161 nm, dose — 6300 kJ/$ m^{2} $). It has been found that the change in the spectral‐fluorescent properties of BSA molecules after irradiation under the conditions of different microsurroundings is caused by the “unrolling” of the protein globule due to the weakening and rupture of weak intramolecular bonds as well as by the photomodification of the aromatic amino acid residues in the composition of the protein macromolecule. A scheme of the phototransformation processes in the BSA molecules under the action of vacuum ultraviolet has been drawn. In accordance with this scheme the VUV light in the region of absorption of peptide bonds of protein molecules induces a disturbance in their third‐order structure, which leads to a modification of the state of aromatic amino acid residues and a change in the functional properties of protein macromolecules. Pantyavin, A. A. aut Vashanov, G. A. aut Enthalten in Journal of applied spectroscopy Kluwer Academic Publishers-Plenum Publishers, 1966 68(2001), 2 vom: März, Seite 291-298 (DE-627)129972495 (DE-600)410515-1 (DE-576)015535800 0021-9037 nnns volume:68 year:2001 number:2 month:03 pages:291-298 https://doi.org/10.1023/A:1019224404819 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-PHY SSG-OLC-CHE GBV_ILN_40 GBV_ILN_70 GBV_ILN_4700 AR 68 2001 2 03 291-298 |
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10.1023/A:1019224404819 doi (DE-627)OLC2034664051 (DE-He213)A:1019224404819-p DE-627 ger DE-627 rakwb eng 530 VZ 11 ssgn Artyukhov, V. G. verfasserin aut Vacuum‐UV‐Radiation‐Induced Structural‐Functional Changes in Serum Albumin Molecules 2001 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Plenum Publishing Corporation 2001 Abstract Using the methods of spectrophotometry, luminescent analysis, and fluorescent probes, we have investigated the structural changes in bull serum albumin (BSA) molecules induced by the action of vacuum UV (VUV) radiation (λ = 131161 nm, dose — 6300 kJ/$ m^{2} $). It has been found that the change in the spectral‐fluorescent properties of BSA molecules after irradiation under the conditions of different microsurroundings is caused by the “unrolling” of the protein globule due to the weakening and rupture of weak intramolecular bonds as well as by the photomodification of the aromatic amino acid residues in the composition of the protein macromolecule. A scheme of the phototransformation processes in the BSA molecules under the action of vacuum ultraviolet has been drawn. In accordance with this scheme the VUV light in the region of absorption of peptide bonds of protein molecules induces a disturbance in their third‐order structure, which leads to a modification of the state of aromatic amino acid residues and a change in the functional properties of protein macromolecules. Pantyavin, A. A. aut Vashanov, G. A. aut Enthalten in Journal of applied spectroscopy Kluwer Academic Publishers-Plenum Publishers, 1966 68(2001), 2 vom: März, Seite 291-298 (DE-627)129972495 (DE-600)410515-1 (DE-576)015535800 0021-9037 nnns volume:68 year:2001 number:2 month:03 pages:291-298 https://doi.org/10.1023/A:1019224404819 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-PHY SSG-OLC-CHE GBV_ILN_40 GBV_ILN_70 GBV_ILN_4700 AR 68 2001 2 03 291-298 |
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10.1023/A:1019224404819 doi (DE-627)OLC2034664051 (DE-He213)A:1019224404819-p DE-627 ger DE-627 rakwb eng 530 VZ 11 ssgn Artyukhov, V. G. verfasserin aut Vacuum‐UV‐Radiation‐Induced Structural‐Functional Changes in Serum Albumin Molecules 2001 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Plenum Publishing Corporation 2001 Abstract Using the methods of spectrophotometry, luminescent analysis, and fluorescent probes, we have investigated the structural changes in bull serum albumin (BSA) molecules induced by the action of vacuum UV (VUV) radiation (λ = 131161 nm, dose — 6300 kJ/$ m^{2} $). It has been found that the change in the spectral‐fluorescent properties of BSA molecules after irradiation under the conditions of different microsurroundings is caused by the “unrolling” of the protein globule due to the weakening and rupture of weak intramolecular bonds as well as by the photomodification of the aromatic amino acid residues in the composition of the protein macromolecule. A scheme of the phototransformation processes in the BSA molecules under the action of vacuum ultraviolet has been drawn. In accordance with this scheme the VUV light in the region of absorption of peptide bonds of protein molecules induces a disturbance in their third‐order structure, which leads to a modification of the state of aromatic amino acid residues and a change in the functional properties of protein macromolecules. Pantyavin, A. A. aut Vashanov, G. A. aut Enthalten in Journal of applied spectroscopy Kluwer Academic Publishers-Plenum Publishers, 1966 68(2001), 2 vom: März, Seite 291-298 (DE-627)129972495 (DE-600)410515-1 (DE-576)015535800 0021-9037 nnns volume:68 year:2001 number:2 month:03 pages:291-298 https://doi.org/10.1023/A:1019224404819 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-PHY SSG-OLC-CHE GBV_ILN_40 GBV_ILN_70 GBV_ILN_4700 AR 68 2001 2 03 291-298 |
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10.1023/A:1019224404819 doi (DE-627)OLC2034664051 (DE-He213)A:1019224404819-p DE-627 ger DE-627 rakwb eng 530 VZ 11 ssgn Artyukhov, V. G. verfasserin aut Vacuum‐UV‐Radiation‐Induced Structural‐Functional Changes in Serum Albumin Molecules 2001 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Plenum Publishing Corporation 2001 Abstract Using the methods of spectrophotometry, luminescent analysis, and fluorescent probes, we have investigated the structural changes in bull serum albumin (BSA) molecules induced by the action of vacuum UV (VUV) radiation (λ = 131161 nm, dose — 6300 kJ/$ m^{2} $). It has been found that the change in the spectral‐fluorescent properties of BSA molecules after irradiation under the conditions of different microsurroundings is caused by the “unrolling” of the protein globule due to the weakening and rupture of weak intramolecular bonds as well as by the photomodification of the aromatic amino acid residues in the composition of the protein macromolecule. A scheme of the phototransformation processes in the BSA molecules under the action of vacuum ultraviolet has been drawn. In accordance with this scheme the VUV light in the region of absorption of peptide bonds of protein molecules induces a disturbance in their third‐order structure, which leads to a modification of the state of aromatic amino acid residues and a change in the functional properties of protein macromolecules. Pantyavin, A. A. aut Vashanov, G. A. aut Enthalten in Journal of applied spectroscopy Kluwer Academic Publishers-Plenum Publishers, 1966 68(2001), 2 vom: März, Seite 291-298 (DE-627)129972495 (DE-600)410515-1 (DE-576)015535800 0021-9037 nnns volume:68 year:2001 number:2 month:03 pages:291-298 https://doi.org/10.1023/A:1019224404819 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-PHY SSG-OLC-CHE GBV_ILN_40 GBV_ILN_70 GBV_ILN_4700 AR 68 2001 2 03 291-298 |
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10.1023/A:1019224404819 doi (DE-627)OLC2034664051 (DE-He213)A:1019224404819-p DE-627 ger DE-627 rakwb eng 530 VZ 11 ssgn Artyukhov, V. G. verfasserin aut Vacuum‐UV‐Radiation‐Induced Structural‐Functional Changes in Serum Albumin Molecules 2001 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Plenum Publishing Corporation 2001 Abstract Using the methods of spectrophotometry, luminescent analysis, and fluorescent probes, we have investigated the structural changes in bull serum albumin (BSA) molecules induced by the action of vacuum UV (VUV) radiation (λ = 131161 nm, dose — 6300 kJ/$ m^{2} $). It has been found that the change in the spectral‐fluorescent properties of BSA molecules after irradiation under the conditions of different microsurroundings is caused by the “unrolling” of the protein globule due to the weakening and rupture of weak intramolecular bonds as well as by the photomodification of the aromatic amino acid residues in the composition of the protein macromolecule. A scheme of the phototransformation processes in the BSA molecules under the action of vacuum ultraviolet has been drawn. In accordance with this scheme the VUV light in the region of absorption of peptide bonds of protein molecules induces a disturbance in their third‐order structure, which leads to a modification of the state of aromatic amino acid residues and a change in the functional properties of protein macromolecules. Pantyavin, A. A. aut Vashanov, G. A. aut Enthalten in Journal of applied spectroscopy Kluwer Academic Publishers-Plenum Publishers, 1966 68(2001), 2 vom: März, Seite 291-298 (DE-627)129972495 (DE-600)410515-1 (DE-576)015535800 0021-9037 nnns volume:68 year:2001 number:2 month:03 pages:291-298 https://doi.org/10.1023/A:1019224404819 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-PHY SSG-OLC-CHE GBV_ILN_40 GBV_ILN_70 GBV_ILN_4700 AR 68 2001 2 03 291-298 |
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Abstract Using the methods of spectrophotometry, luminescent analysis, and fluorescent probes, we have investigated the structural changes in bull serum albumin (BSA) molecules induced by the action of vacuum UV (VUV) radiation (λ = 131161 nm, dose — 6300 kJ/$ m^{2} $). It has been found that the change in the spectral‐fluorescent properties of BSA molecules after irradiation under the conditions of different microsurroundings is caused by the “unrolling” of the protein globule due to the weakening and rupture of weak intramolecular bonds as well as by the photomodification of the aromatic amino acid residues in the composition of the protein macromolecule. A scheme of the phototransformation processes in the BSA molecules under the action of vacuum ultraviolet has been drawn. In accordance with this scheme the VUV light in the region of absorption of peptide bonds of protein molecules induces a disturbance in their third‐order structure, which leads to a modification of the state of aromatic amino acid residues and a change in the functional properties of protein macromolecules. © Plenum Publishing Corporation 2001 |
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Abstract Using the methods of spectrophotometry, luminescent analysis, and fluorescent probes, we have investigated the structural changes in bull serum albumin (BSA) molecules induced by the action of vacuum UV (VUV) radiation (λ = 131161 nm, dose — 6300 kJ/$ m^{2} $). It has been found that the change in the spectral‐fluorescent properties of BSA molecules after irradiation under the conditions of different microsurroundings is caused by the “unrolling” of the protein globule due to the weakening and rupture of weak intramolecular bonds as well as by the photomodification of the aromatic amino acid residues in the composition of the protein macromolecule. A scheme of the phototransformation processes in the BSA molecules under the action of vacuum ultraviolet has been drawn. In accordance with this scheme the VUV light in the region of absorption of peptide bonds of protein molecules induces a disturbance in their third‐order structure, which leads to a modification of the state of aromatic amino acid residues and a change in the functional properties of protein macromolecules. © Plenum Publishing Corporation 2001 |
| abstract_unstemmed |
Abstract Using the methods of spectrophotometry, luminescent analysis, and fluorescent probes, we have investigated the structural changes in bull serum albumin (BSA) molecules induced by the action of vacuum UV (VUV) radiation (λ = 131161 nm, dose — 6300 kJ/$ m^{2} $). It has been found that the change in the spectral‐fluorescent properties of BSA molecules after irradiation under the conditions of different microsurroundings is caused by the “unrolling” of the protein globule due to the weakening and rupture of weak intramolecular bonds as well as by the photomodification of the aromatic amino acid residues in the composition of the protein macromolecule. A scheme of the phototransformation processes in the BSA molecules under the action of vacuum ultraviolet has been drawn. In accordance with this scheme the VUV light in the region of absorption of peptide bonds of protein molecules induces a disturbance in their third‐order structure, which leads to a modification of the state of aromatic amino acid residues and a change in the functional properties of protein macromolecules. © Plenum Publishing Corporation 2001 |
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Pantyavin, A. A. Vashanov, G. A. |
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Pantyavin, A. A. Vashanov, G. A. |
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| doi_str |
10.1023/A:1019224404819 |
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2024-07-03T21:55:33.267Z |
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G.</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Vacuum‐UV‐Radiation‐Induced Structural‐Functional Changes in Serum Albumin Molecules</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">2001</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">Text</subfield><subfield code="b">txt</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">ohne Hilfsmittel zu benutzen</subfield><subfield code="b">n</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">Band</subfield><subfield code="b">nc</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="500" ind1=" " ind2=" "><subfield code="a">© Plenum Publishing Corporation 2001</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Abstract Using the methods of spectrophotometry, luminescent analysis, and fluorescent probes, we have investigated the structural changes in bull serum albumin (BSA) molecules induced by the action of vacuum UV (VUV) radiation (λ = 131161 nm, dose — 6300 kJ/$ m^{2} $). 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