Secondary structural changes of large and small fragments of bovine serum albumin in thermal denaturation and in sodium dodecyl sulfate denaturation
Abstract The helicities in various fragments of bovine serum albumin (BSA) were examined in the thermal denaturation and in sodium docecyl sulfate (SDS) denaturation. The thermal denaturation was examined in a temperature range between 2 and 65°C. The helicity decreased with a rise of temperature an...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Takeda, Kunio [verfasserIn] |
|---|
| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
1993 |
|---|
| Anmerkung: |
© Plenum Publishing Corporation 1993 |
|---|
| Übergeordnetes Werk: |
Enthalten in: The protein journal - Dordrecht : Springer Science + Business Media B.V., 2004, 12(1993), 2 vom: 01. Apr., Seite 223-228 |
|---|---|
| Übergeordnetes Werk: |
volume:12 ; year:1993 ; number:2 ; day:01 ; month:04 ; pages:223-228 |
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10.1007/BF01026044 |
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| 520 | |a Abstract The helicities in various fragments of bovine serum albumin (BSA) were examined in the thermal denaturation and in sodium docecyl sulfate (SDS) denaturation. The thermal denaturation was examined in a temperature range between 2 and 65°C. The helicity decreased with a rise of temperature and it recovered to some degree upon cooling temperature. A rather high reversibility was observed in the BSA fragments, which were located in the N-terminal of the parent protein and then contained the first large loop with no disulfide bridge. The high reversibility was available also for the helicity in the first large loop of the fragment, disulfide bridges of which were reduced. The fragments, which were smaller than one domain, became unstable in the SDS denaturation. The helicities of such fragments decreased in lower SDS concentrations compared with those of the intact BSA and the large fragments, which contained one or more domains. A resistance to the SDS denaturation appeared in the helices of every large loop even after the fragmentation. On the other hand, helicities of the fragments decreased to 20–25% upon the reduction of disulfide bridges. However, the helicities of these fragments increased to 35–40% in the SDS denaturation. | ||
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10.1007/BF01026044 doi (DE-627)SPR052804526 (SPR)BF01026044-e DE-627 ger DE-627 rakwb eng Takeda, Kunio verfasserin aut Secondary structural changes of large and small fragments of bovine serum albumin in thermal denaturation and in sodium dodecyl sulfate denaturation 1993 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Plenum Publishing Corporation 1993 Abstract The helicities in various fragments of bovine serum albumin (BSA) were examined in the thermal denaturation and in sodium docecyl sulfate (SDS) denaturation. The thermal denaturation was examined in a temperature range between 2 and 65°C. The helicity decreased with a rise of temperature and it recovered to some degree upon cooling temperature. A rather high reversibility was observed in the BSA fragments, which were located in the N-terminal of the parent protein and then contained the first large loop with no disulfide bridge. The high reversibility was available also for the helicity in the first large loop of the fragment, disulfide bridges of which were reduced. The fragments, which were smaller than one domain, became unstable in the SDS denaturation. The helicities of such fragments decreased in lower SDS concentrations compared with those of the intact BSA and the large fragments, which contained one or more domains. A resistance to the SDS denaturation appeared in the helices of every large loop even after the fragmentation. On the other hand, helicities of the fragments decreased to 20–25% upon the reduction of disulfide bridges. However, the helicities of these fragments increased to 35–40% in the SDS denaturation. Hamada, Satoshi aut Wada, Akira aut Enthalten in The protein journal Dordrecht : Springer Science + Business Media B.V., 2004 12(1993), 2 vom: 01. Apr., Seite 223-228 (DE-627)385615884 (DE-600)2143071-8 1573-4943 nnns volume:12 year:1993 number:2 day:01 month:04 pages:223-228 https://dx.doi.org/10.1007/BF01026044 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER GBV_ILN_150 GBV_ILN_2048 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2110 GBV_ILN_4367 AR 12 1993 2 01 04 223-228 |
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10.1007/BF01026044 doi (DE-627)SPR052804526 (SPR)BF01026044-e DE-627 ger DE-627 rakwb eng Takeda, Kunio verfasserin aut Secondary structural changes of large and small fragments of bovine serum albumin in thermal denaturation and in sodium dodecyl sulfate denaturation 1993 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Plenum Publishing Corporation 1993 Abstract The helicities in various fragments of bovine serum albumin (BSA) were examined in the thermal denaturation and in sodium docecyl sulfate (SDS) denaturation. The thermal denaturation was examined in a temperature range between 2 and 65°C. The helicity decreased with a rise of temperature and it recovered to some degree upon cooling temperature. A rather high reversibility was observed in the BSA fragments, which were located in the N-terminal of the parent protein and then contained the first large loop with no disulfide bridge. The high reversibility was available also for the helicity in the first large loop of the fragment, disulfide bridges of which were reduced. The fragments, which were smaller than one domain, became unstable in the SDS denaturation. The helicities of such fragments decreased in lower SDS concentrations compared with those of the intact BSA and the large fragments, which contained one or more domains. A resistance to the SDS denaturation appeared in the helices of every large loop even after the fragmentation. On the other hand, helicities of the fragments decreased to 20–25% upon the reduction of disulfide bridges. However, the helicities of these fragments increased to 35–40% in the SDS denaturation. Hamada, Satoshi aut Wada, Akira aut Enthalten in The protein journal Dordrecht : Springer Science + Business Media B.V., 2004 12(1993), 2 vom: 01. Apr., Seite 223-228 (DE-627)385615884 (DE-600)2143071-8 1573-4943 nnns volume:12 year:1993 number:2 day:01 month:04 pages:223-228 https://dx.doi.org/10.1007/BF01026044 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER GBV_ILN_150 GBV_ILN_2048 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2110 GBV_ILN_4367 AR 12 1993 2 01 04 223-228 |
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10.1007/BF01026044 doi (DE-627)SPR052804526 (SPR)BF01026044-e DE-627 ger DE-627 rakwb eng Takeda, Kunio verfasserin aut Secondary structural changes of large and small fragments of bovine serum albumin in thermal denaturation and in sodium dodecyl sulfate denaturation 1993 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Plenum Publishing Corporation 1993 Abstract The helicities in various fragments of bovine serum albumin (BSA) were examined in the thermal denaturation and in sodium docecyl sulfate (SDS) denaturation. The thermal denaturation was examined in a temperature range between 2 and 65°C. The helicity decreased with a rise of temperature and it recovered to some degree upon cooling temperature. A rather high reversibility was observed in the BSA fragments, which were located in the N-terminal of the parent protein and then contained the first large loop with no disulfide bridge. The high reversibility was available also for the helicity in the first large loop of the fragment, disulfide bridges of which were reduced. The fragments, which were smaller than one domain, became unstable in the SDS denaturation. The helicities of such fragments decreased in lower SDS concentrations compared with those of the intact BSA and the large fragments, which contained one or more domains. A resistance to the SDS denaturation appeared in the helices of every large loop even after the fragmentation. On the other hand, helicities of the fragments decreased to 20–25% upon the reduction of disulfide bridges. However, the helicities of these fragments increased to 35–40% in the SDS denaturation. Hamada, Satoshi aut Wada, Akira aut Enthalten in The protein journal Dordrecht : Springer Science + Business Media B.V., 2004 12(1993), 2 vom: 01. Apr., Seite 223-228 (DE-627)385615884 (DE-600)2143071-8 1573-4943 nnns volume:12 year:1993 number:2 day:01 month:04 pages:223-228 https://dx.doi.org/10.1007/BF01026044 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER GBV_ILN_150 GBV_ILN_2048 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2110 GBV_ILN_4367 AR 12 1993 2 01 04 223-228 |
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10.1007/BF01026044 doi (DE-627)SPR052804526 (SPR)BF01026044-e DE-627 ger DE-627 rakwb eng Takeda, Kunio verfasserin aut Secondary structural changes of large and small fragments of bovine serum albumin in thermal denaturation and in sodium dodecyl sulfate denaturation 1993 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Plenum Publishing Corporation 1993 Abstract The helicities in various fragments of bovine serum albumin (BSA) were examined in the thermal denaturation and in sodium docecyl sulfate (SDS) denaturation. The thermal denaturation was examined in a temperature range between 2 and 65°C. The helicity decreased with a rise of temperature and it recovered to some degree upon cooling temperature. A rather high reversibility was observed in the BSA fragments, which were located in the N-terminal of the parent protein and then contained the first large loop with no disulfide bridge. The high reversibility was available also for the helicity in the first large loop of the fragment, disulfide bridges of which were reduced. The fragments, which were smaller than one domain, became unstable in the SDS denaturation. The helicities of such fragments decreased in lower SDS concentrations compared with those of the intact BSA and the large fragments, which contained one or more domains. A resistance to the SDS denaturation appeared in the helices of every large loop even after the fragmentation. On the other hand, helicities of the fragments decreased to 20–25% upon the reduction of disulfide bridges. However, the helicities of these fragments increased to 35–40% in the SDS denaturation. Hamada, Satoshi aut Wada, Akira aut Enthalten in The protein journal Dordrecht : Springer Science + Business Media B.V., 2004 12(1993), 2 vom: 01. Apr., Seite 223-228 (DE-627)385615884 (DE-600)2143071-8 1573-4943 nnns volume:12 year:1993 number:2 day:01 month:04 pages:223-228 https://dx.doi.org/10.1007/BF01026044 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER GBV_ILN_150 GBV_ILN_2048 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2110 GBV_ILN_4367 AR 12 1993 2 01 04 223-228 |
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10.1007/BF01026044 doi (DE-627)SPR052804526 (SPR)BF01026044-e DE-627 ger DE-627 rakwb eng Takeda, Kunio verfasserin aut Secondary structural changes of large and small fragments of bovine serum albumin in thermal denaturation and in sodium dodecyl sulfate denaturation 1993 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Plenum Publishing Corporation 1993 Abstract The helicities in various fragments of bovine serum albumin (BSA) were examined in the thermal denaturation and in sodium docecyl sulfate (SDS) denaturation. The thermal denaturation was examined in a temperature range between 2 and 65°C. The helicity decreased with a rise of temperature and it recovered to some degree upon cooling temperature. A rather high reversibility was observed in the BSA fragments, which were located in the N-terminal of the parent protein and then contained the first large loop with no disulfide bridge. The high reversibility was available also for the helicity in the first large loop of the fragment, disulfide bridges of which were reduced. The fragments, which were smaller than one domain, became unstable in the SDS denaturation. The helicities of such fragments decreased in lower SDS concentrations compared with those of the intact BSA and the large fragments, which contained one or more domains. A resistance to the SDS denaturation appeared in the helices of every large loop even after the fragmentation. On the other hand, helicities of the fragments decreased to 20–25% upon the reduction of disulfide bridges. However, the helicities of these fragments increased to 35–40% in the SDS denaturation. Hamada, Satoshi aut Wada, Akira aut Enthalten in The protein journal Dordrecht : Springer Science + Business Media B.V., 2004 12(1993), 2 vom: 01. Apr., Seite 223-228 (DE-627)385615884 (DE-600)2143071-8 1573-4943 nnns volume:12 year:1993 number:2 day:01 month:04 pages:223-228 https://dx.doi.org/10.1007/BF01026044 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER GBV_ILN_150 GBV_ILN_2048 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2110 GBV_ILN_4367 AR 12 1993 2 01 04 223-228 |
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secondary structural changes of large and small fragments of bovine serum albumin in thermal denaturation and in sodium dodecyl sulfate denaturation |
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Secondary structural changes of large and small fragments of bovine serum albumin in thermal denaturation and in sodium dodecyl sulfate denaturation |
| abstract |
Abstract The helicities in various fragments of bovine serum albumin (BSA) were examined in the thermal denaturation and in sodium docecyl sulfate (SDS) denaturation. The thermal denaturation was examined in a temperature range between 2 and 65°C. The helicity decreased with a rise of temperature and it recovered to some degree upon cooling temperature. A rather high reversibility was observed in the BSA fragments, which were located in the N-terminal of the parent protein and then contained the first large loop with no disulfide bridge. The high reversibility was available also for the helicity in the first large loop of the fragment, disulfide bridges of which were reduced. The fragments, which were smaller than one domain, became unstable in the SDS denaturation. The helicities of such fragments decreased in lower SDS concentrations compared with those of the intact BSA and the large fragments, which contained one or more domains. A resistance to the SDS denaturation appeared in the helices of every large loop even after the fragmentation. On the other hand, helicities of the fragments decreased to 20–25% upon the reduction of disulfide bridges. However, the helicities of these fragments increased to 35–40% in the SDS denaturation. © Plenum Publishing Corporation 1993 |
| abstractGer |
Abstract The helicities in various fragments of bovine serum albumin (BSA) were examined in the thermal denaturation and in sodium docecyl sulfate (SDS) denaturation. The thermal denaturation was examined in a temperature range between 2 and 65°C. The helicity decreased with a rise of temperature and it recovered to some degree upon cooling temperature. A rather high reversibility was observed in the BSA fragments, which were located in the N-terminal of the parent protein and then contained the first large loop with no disulfide bridge. The high reversibility was available also for the helicity in the first large loop of the fragment, disulfide bridges of which were reduced. The fragments, which were smaller than one domain, became unstable in the SDS denaturation. The helicities of such fragments decreased in lower SDS concentrations compared with those of the intact BSA and the large fragments, which contained one or more domains. A resistance to the SDS denaturation appeared in the helices of every large loop even after the fragmentation. On the other hand, helicities of the fragments decreased to 20–25% upon the reduction of disulfide bridges. However, the helicities of these fragments increased to 35–40% in the SDS denaturation. © Plenum Publishing Corporation 1993 |
| abstract_unstemmed |
Abstract The helicities in various fragments of bovine serum albumin (BSA) were examined in the thermal denaturation and in sodium docecyl sulfate (SDS) denaturation. The thermal denaturation was examined in a temperature range between 2 and 65°C. The helicity decreased with a rise of temperature and it recovered to some degree upon cooling temperature. A rather high reversibility was observed in the BSA fragments, which were located in the N-terminal of the parent protein and then contained the first large loop with no disulfide bridge. The high reversibility was available also for the helicity in the first large loop of the fragment, disulfide bridges of which were reduced. The fragments, which were smaller than one domain, became unstable in the SDS denaturation. The helicities of such fragments decreased in lower SDS concentrations compared with those of the intact BSA and the large fragments, which contained one or more domains. A resistance to the SDS denaturation appeared in the helices of every large loop even after the fragmentation. On the other hand, helicities of the fragments decreased to 20–25% upon the reduction of disulfide bridges. However, the helicities of these fragments increased to 35–40% in the SDS denaturation. © Plenum Publishing Corporation 1993 |
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10.1007/BF01026044 |
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