Biochemical analysis of a Chinese cabbage phytocystatin-1
Abstract The phytocystatins are inhibitors of papain-like cysteine proteinases that are implicated in defense mechanisms and the regulation of protein turnover. BCPI-1, a Brassica rapa (Chinese cabbage) phytocystatin isolated from flower buds, contains an extended C-terminal region that contains a s...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Hong, Joon Ki [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2011 |
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| Schlagwörter: |
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| Anmerkung: |
© The Genetics Society of Korea and Springer Netherlands 2012 |
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| Übergeordnetes Werk: |
Enthalten in: Genes & Genomics - The Genetics Society of Korea, 2010, 34(2011), 1 vom: 30. Dez., Seite 13-18 |
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| Übergeordnetes Werk: |
volume:34 ; year:2011 ; number:1 ; day:30 ; month:12 ; pages:13-18 |
| Links: |
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| DOI / URN: |
10.1007/s13258-011-0150-x |
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| 520 | |a Abstract The phytocystatins are inhibitors of papain-like cysteine proteinases that are implicated in defense mechanisms and the regulation of protein turnover. BCPI-1, a Brassica rapa (Chinese cabbage) phytocystatin isolated from flower buds, contains an extended C-terminal region that contains a single Cys residue at position 102. In an effort to investigate the role of the C-terminus and this Cys residue in BCPI-1 activity, purified recombinant proteins of BCPI-1, including wild-type BCPI-1 (wtBCPI-1), N-terminus BCPI-1 (BCPI-1ΔC), C-terminus BCPI-1 (BCPI-1ΔN), and BCPI-1 with a single Cys residue exchange to Ser (BCPI-1C102S), were generated and their inhibitory activities against papain were investigated. Kinetic analysis revealed that the monomeric forms of wtBCPI-1 (Ki = 6.84 ± 0.3 × $ 10^{−8} $ M) inhibited papain more efficiently than the dimeric forms of wtBCPI-1 (Ki = 1.01 ± 0.5 × $ 10^{−7} $ M). Experiments with recombinant BCPI-1C102S demonstrated that the dimerization of wtBCPI-1 caused by the formation of an intermolecular disulfide bond at the cysteine residue. The inhibitory activity of the recombinant proteins, except BCPI-1ΔN, was reduced in the pH range of 7.0–11.5 and was highly stable over a wide range of temperatures. Thus, dimerization mediated by the cysteine residue in the extended C-terminal region and alkaline conditions reduced the inhibitory activity of BCPI-1. | ||
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10.1007/s13258-011-0150-x doi (DE-627)SPR031098444 (SPR)s13258-011-0150-x-e DE-627 ger DE-627 rakwb eng Hong, Joon Ki verfasserin aut Biochemical analysis of a Chinese cabbage phytocystatin-1 2011 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Genetics Society of Korea and Springer Netherlands 2012 Abstract The phytocystatins are inhibitors of papain-like cysteine proteinases that are implicated in defense mechanisms and the regulation of protein turnover. BCPI-1, a Brassica rapa (Chinese cabbage) phytocystatin isolated from flower buds, contains an extended C-terminal region that contains a single Cys residue at position 102. In an effort to investigate the role of the C-terminus and this Cys residue in BCPI-1 activity, purified recombinant proteins of BCPI-1, including wild-type BCPI-1 (wtBCPI-1), N-terminus BCPI-1 (BCPI-1ΔC), C-terminus BCPI-1 (BCPI-1ΔN), and BCPI-1 with a single Cys residue exchange to Ser (BCPI-1C102S), were generated and their inhibitory activities against papain were investigated. Kinetic analysis revealed that the monomeric forms of wtBCPI-1 (Ki = 6.84 ± 0.3 × $ 10^{−8} $ M) inhibited papain more efficiently than the dimeric forms of wtBCPI-1 (Ki = 1.01 ± 0.5 × $ 10^{−7} $ M). Experiments with recombinant BCPI-1C102S demonstrated that the dimerization of wtBCPI-1 caused by the formation of an intermolecular disulfide bond at the cysteine residue. The inhibitory activity of the recombinant proteins, except BCPI-1ΔN, was reduced in the pH range of 7.0–11.5 and was highly stable over a wide range of temperatures. Thus, dimerization mediated by the cysteine residue in the extended C-terminal region and alkaline conditions reduced the inhibitory activity of BCPI-1. Inhibitory activity (dpeaa)DE-He213 Protein kinetics (dpeaa)DE-He213 Protein stability (dpeaa)DE-He213 Recombinant proteins (dpeaa)DE-He213 Je, Jihyun aut Song, Chieun aut Hwang, Jung Eun aut Lee, Yeon-Hee aut Lim, Chae Oh aut Enthalten in Genes & Genomics The Genetics Society of Korea, 2010 34(2011), 1 vom: 30. Dez., Seite 13-18 (DE-627)SPR031096425 nnns volume:34 year:2011 number:1 day:30 month:12 pages:13-18 https://dx.doi.org/10.1007/s13258-011-0150-x lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER AR 34 2011 1 30 12 13-18 |
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10.1007/s13258-011-0150-x doi (DE-627)SPR031098444 (SPR)s13258-011-0150-x-e DE-627 ger DE-627 rakwb eng Hong, Joon Ki verfasserin aut Biochemical analysis of a Chinese cabbage phytocystatin-1 2011 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Genetics Society of Korea and Springer Netherlands 2012 Abstract The phytocystatins are inhibitors of papain-like cysteine proteinases that are implicated in defense mechanisms and the regulation of protein turnover. BCPI-1, a Brassica rapa (Chinese cabbage) phytocystatin isolated from flower buds, contains an extended C-terminal region that contains a single Cys residue at position 102. In an effort to investigate the role of the C-terminus and this Cys residue in BCPI-1 activity, purified recombinant proteins of BCPI-1, including wild-type BCPI-1 (wtBCPI-1), N-terminus BCPI-1 (BCPI-1ΔC), C-terminus BCPI-1 (BCPI-1ΔN), and BCPI-1 with a single Cys residue exchange to Ser (BCPI-1C102S), were generated and their inhibitory activities against papain were investigated. Kinetic analysis revealed that the monomeric forms of wtBCPI-1 (Ki = 6.84 ± 0.3 × $ 10^{−8} $ M) inhibited papain more efficiently than the dimeric forms of wtBCPI-1 (Ki = 1.01 ± 0.5 × $ 10^{−7} $ M). Experiments with recombinant BCPI-1C102S demonstrated that the dimerization of wtBCPI-1 caused by the formation of an intermolecular disulfide bond at the cysteine residue. The inhibitory activity of the recombinant proteins, except BCPI-1ΔN, was reduced in the pH range of 7.0–11.5 and was highly stable over a wide range of temperatures. Thus, dimerization mediated by the cysteine residue in the extended C-terminal region and alkaline conditions reduced the inhibitory activity of BCPI-1. Inhibitory activity (dpeaa)DE-He213 Protein kinetics (dpeaa)DE-He213 Protein stability (dpeaa)DE-He213 Recombinant proteins (dpeaa)DE-He213 Je, Jihyun aut Song, Chieun aut Hwang, Jung Eun aut Lee, Yeon-Hee aut Lim, Chae Oh aut Enthalten in Genes & Genomics The Genetics Society of Korea, 2010 34(2011), 1 vom: 30. Dez., Seite 13-18 (DE-627)SPR031096425 nnns volume:34 year:2011 number:1 day:30 month:12 pages:13-18 https://dx.doi.org/10.1007/s13258-011-0150-x lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER AR 34 2011 1 30 12 13-18 |
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10.1007/s13258-011-0150-x doi (DE-627)SPR031098444 (SPR)s13258-011-0150-x-e DE-627 ger DE-627 rakwb eng Hong, Joon Ki verfasserin aut Biochemical analysis of a Chinese cabbage phytocystatin-1 2011 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Genetics Society of Korea and Springer Netherlands 2012 Abstract The phytocystatins are inhibitors of papain-like cysteine proteinases that are implicated in defense mechanisms and the regulation of protein turnover. BCPI-1, a Brassica rapa (Chinese cabbage) phytocystatin isolated from flower buds, contains an extended C-terminal region that contains a single Cys residue at position 102. In an effort to investigate the role of the C-terminus and this Cys residue in BCPI-1 activity, purified recombinant proteins of BCPI-1, including wild-type BCPI-1 (wtBCPI-1), N-terminus BCPI-1 (BCPI-1ΔC), C-terminus BCPI-1 (BCPI-1ΔN), and BCPI-1 with a single Cys residue exchange to Ser (BCPI-1C102S), were generated and their inhibitory activities against papain were investigated. Kinetic analysis revealed that the monomeric forms of wtBCPI-1 (Ki = 6.84 ± 0.3 × $ 10^{−8} $ M) inhibited papain more efficiently than the dimeric forms of wtBCPI-1 (Ki = 1.01 ± 0.5 × $ 10^{−7} $ M). Experiments with recombinant BCPI-1C102S demonstrated that the dimerization of wtBCPI-1 caused by the formation of an intermolecular disulfide bond at the cysteine residue. The inhibitory activity of the recombinant proteins, except BCPI-1ΔN, was reduced in the pH range of 7.0–11.5 and was highly stable over a wide range of temperatures. Thus, dimerization mediated by the cysteine residue in the extended C-terminal region and alkaline conditions reduced the inhibitory activity of BCPI-1. Inhibitory activity (dpeaa)DE-He213 Protein kinetics (dpeaa)DE-He213 Protein stability (dpeaa)DE-He213 Recombinant proteins (dpeaa)DE-He213 Je, Jihyun aut Song, Chieun aut Hwang, Jung Eun aut Lee, Yeon-Hee aut Lim, Chae Oh aut Enthalten in Genes & Genomics The Genetics Society of Korea, 2010 34(2011), 1 vom: 30. Dez., Seite 13-18 (DE-627)SPR031096425 nnns volume:34 year:2011 number:1 day:30 month:12 pages:13-18 https://dx.doi.org/10.1007/s13258-011-0150-x lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER AR 34 2011 1 30 12 13-18 |
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10.1007/s13258-011-0150-x doi (DE-627)SPR031098444 (SPR)s13258-011-0150-x-e DE-627 ger DE-627 rakwb eng Hong, Joon Ki verfasserin aut Biochemical analysis of a Chinese cabbage phytocystatin-1 2011 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Genetics Society of Korea and Springer Netherlands 2012 Abstract The phytocystatins are inhibitors of papain-like cysteine proteinases that are implicated in defense mechanisms and the regulation of protein turnover. BCPI-1, a Brassica rapa (Chinese cabbage) phytocystatin isolated from flower buds, contains an extended C-terminal region that contains a single Cys residue at position 102. In an effort to investigate the role of the C-terminus and this Cys residue in BCPI-1 activity, purified recombinant proteins of BCPI-1, including wild-type BCPI-1 (wtBCPI-1), N-terminus BCPI-1 (BCPI-1ΔC), C-terminus BCPI-1 (BCPI-1ΔN), and BCPI-1 with a single Cys residue exchange to Ser (BCPI-1C102S), were generated and their inhibitory activities against papain were investigated. Kinetic analysis revealed that the monomeric forms of wtBCPI-1 (Ki = 6.84 ± 0.3 × $ 10^{−8} $ M) inhibited papain more efficiently than the dimeric forms of wtBCPI-1 (Ki = 1.01 ± 0.5 × $ 10^{−7} $ M). Experiments with recombinant BCPI-1C102S demonstrated that the dimerization of wtBCPI-1 caused by the formation of an intermolecular disulfide bond at the cysteine residue. The inhibitory activity of the recombinant proteins, except BCPI-1ΔN, was reduced in the pH range of 7.0–11.5 and was highly stable over a wide range of temperatures. Thus, dimerization mediated by the cysteine residue in the extended C-terminal region and alkaline conditions reduced the inhibitory activity of BCPI-1. Inhibitory activity (dpeaa)DE-He213 Protein kinetics (dpeaa)DE-He213 Protein stability (dpeaa)DE-He213 Recombinant proteins (dpeaa)DE-He213 Je, Jihyun aut Song, Chieun aut Hwang, Jung Eun aut Lee, Yeon-Hee aut Lim, Chae Oh aut Enthalten in Genes & Genomics The Genetics Society of Korea, 2010 34(2011), 1 vom: 30. Dez., Seite 13-18 (DE-627)SPR031096425 nnns volume:34 year:2011 number:1 day:30 month:12 pages:13-18 https://dx.doi.org/10.1007/s13258-011-0150-x lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER AR 34 2011 1 30 12 13-18 |
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10.1007/s13258-011-0150-x doi (DE-627)SPR031098444 (SPR)s13258-011-0150-x-e DE-627 ger DE-627 rakwb eng Hong, Joon Ki verfasserin aut Biochemical analysis of a Chinese cabbage phytocystatin-1 2011 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Genetics Society of Korea and Springer Netherlands 2012 Abstract The phytocystatins are inhibitors of papain-like cysteine proteinases that are implicated in defense mechanisms and the regulation of protein turnover. BCPI-1, a Brassica rapa (Chinese cabbage) phytocystatin isolated from flower buds, contains an extended C-terminal region that contains a single Cys residue at position 102. In an effort to investigate the role of the C-terminus and this Cys residue in BCPI-1 activity, purified recombinant proteins of BCPI-1, including wild-type BCPI-1 (wtBCPI-1), N-terminus BCPI-1 (BCPI-1ΔC), C-terminus BCPI-1 (BCPI-1ΔN), and BCPI-1 with a single Cys residue exchange to Ser (BCPI-1C102S), were generated and their inhibitory activities against papain were investigated. Kinetic analysis revealed that the monomeric forms of wtBCPI-1 (Ki = 6.84 ± 0.3 × $ 10^{−8} $ M) inhibited papain more efficiently than the dimeric forms of wtBCPI-1 (Ki = 1.01 ± 0.5 × $ 10^{−7} $ M). Experiments with recombinant BCPI-1C102S demonstrated that the dimerization of wtBCPI-1 caused by the formation of an intermolecular disulfide bond at the cysteine residue. The inhibitory activity of the recombinant proteins, except BCPI-1ΔN, was reduced in the pH range of 7.0–11.5 and was highly stable over a wide range of temperatures. Thus, dimerization mediated by the cysteine residue in the extended C-terminal region and alkaline conditions reduced the inhibitory activity of BCPI-1. Inhibitory activity (dpeaa)DE-He213 Protein kinetics (dpeaa)DE-He213 Protein stability (dpeaa)DE-He213 Recombinant proteins (dpeaa)DE-He213 Je, Jihyun aut Song, Chieun aut Hwang, Jung Eun aut Lee, Yeon-Hee aut Lim, Chae Oh aut Enthalten in Genes & Genomics The Genetics Society of Korea, 2010 34(2011), 1 vom: 30. Dez., Seite 13-18 (DE-627)SPR031096425 nnns volume:34 year:2011 number:1 day:30 month:12 pages:13-18 https://dx.doi.org/10.1007/s13258-011-0150-x lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER AR 34 2011 1 30 12 13-18 |
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Hong, Joon Ki Je, Jihyun Song, Chieun Hwang, Jung Eun Lee, Yeon-Hee Lim, Chae Oh |
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34 |
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Elektronische Aufsätze |
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Hong, Joon Ki |
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10.1007/s13258-011-0150-x |
| title_sort |
biochemical analysis of a chinese cabbage phytocystatin-1 |
| title_auth |
Biochemical analysis of a Chinese cabbage phytocystatin-1 |
| abstract |
Abstract The phytocystatins are inhibitors of papain-like cysteine proteinases that are implicated in defense mechanisms and the regulation of protein turnover. BCPI-1, a Brassica rapa (Chinese cabbage) phytocystatin isolated from flower buds, contains an extended C-terminal region that contains a single Cys residue at position 102. In an effort to investigate the role of the C-terminus and this Cys residue in BCPI-1 activity, purified recombinant proteins of BCPI-1, including wild-type BCPI-1 (wtBCPI-1), N-terminus BCPI-1 (BCPI-1ΔC), C-terminus BCPI-1 (BCPI-1ΔN), and BCPI-1 with a single Cys residue exchange to Ser (BCPI-1C102S), were generated and their inhibitory activities against papain were investigated. Kinetic analysis revealed that the monomeric forms of wtBCPI-1 (Ki = 6.84 ± 0.3 × $ 10^{−8} $ M) inhibited papain more efficiently than the dimeric forms of wtBCPI-1 (Ki = 1.01 ± 0.5 × $ 10^{−7} $ M). Experiments with recombinant BCPI-1C102S demonstrated that the dimerization of wtBCPI-1 caused by the formation of an intermolecular disulfide bond at the cysteine residue. The inhibitory activity of the recombinant proteins, except BCPI-1ΔN, was reduced in the pH range of 7.0–11.5 and was highly stable over a wide range of temperatures. Thus, dimerization mediated by the cysteine residue in the extended C-terminal region and alkaline conditions reduced the inhibitory activity of BCPI-1. © The Genetics Society of Korea and Springer Netherlands 2012 |
| abstractGer |
Abstract The phytocystatins are inhibitors of papain-like cysteine proteinases that are implicated in defense mechanisms and the regulation of protein turnover. BCPI-1, a Brassica rapa (Chinese cabbage) phytocystatin isolated from flower buds, contains an extended C-terminal region that contains a single Cys residue at position 102. In an effort to investigate the role of the C-terminus and this Cys residue in BCPI-1 activity, purified recombinant proteins of BCPI-1, including wild-type BCPI-1 (wtBCPI-1), N-terminus BCPI-1 (BCPI-1ΔC), C-terminus BCPI-1 (BCPI-1ΔN), and BCPI-1 with a single Cys residue exchange to Ser (BCPI-1C102S), were generated and their inhibitory activities against papain were investigated. Kinetic analysis revealed that the monomeric forms of wtBCPI-1 (Ki = 6.84 ± 0.3 × $ 10^{−8} $ M) inhibited papain more efficiently than the dimeric forms of wtBCPI-1 (Ki = 1.01 ± 0.5 × $ 10^{−7} $ M). Experiments with recombinant BCPI-1C102S demonstrated that the dimerization of wtBCPI-1 caused by the formation of an intermolecular disulfide bond at the cysteine residue. The inhibitory activity of the recombinant proteins, except BCPI-1ΔN, was reduced in the pH range of 7.0–11.5 and was highly stable over a wide range of temperatures. Thus, dimerization mediated by the cysteine residue in the extended C-terminal region and alkaline conditions reduced the inhibitory activity of BCPI-1. © The Genetics Society of Korea and Springer Netherlands 2012 |
| abstract_unstemmed |
Abstract The phytocystatins are inhibitors of papain-like cysteine proteinases that are implicated in defense mechanisms and the regulation of protein turnover. BCPI-1, a Brassica rapa (Chinese cabbage) phytocystatin isolated from flower buds, contains an extended C-terminal region that contains a single Cys residue at position 102. In an effort to investigate the role of the C-terminus and this Cys residue in BCPI-1 activity, purified recombinant proteins of BCPI-1, including wild-type BCPI-1 (wtBCPI-1), N-terminus BCPI-1 (BCPI-1ΔC), C-terminus BCPI-1 (BCPI-1ΔN), and BCPI-1 with a single Cys residue exchange to Ser (BCPI-1C102S), were generated and their inhibitory activities against papain were investigated. Kinetic analysis revealed that the monomeric forms of wtBCPI-1 (Ki = 6.84 ± 0.3 × $ 10^{−8} $ M) inhibited papain more efficiently than the dimeric forms of wtBCPI-1 (Ki = 1.01 ± 0.5 × $ 10^{−7} $ M). Experiments with recombinant BCPI-1C102S demonstrated that the dimerization of wtBCPI-1 caused by the formation of an intermolecular disulfide bond at the cysteine residue. The inhibitory activity of the recombinant proteins, except BCPI-1ΔN, was reduced in the pH range of 7.0–11.5 and was highly stable over a wide range of temperatures. Thus, dimerization mediated by the cysteine residue in the extended C-terminal region and alkaline conditions reduced the inhibitory activity of BCPI-1. © The Genetics Society of Korea and Springer Netherlands 2012 |
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Biochemical analysis of a Chinese cabbage phytocystatin-1 |
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Je, Jihyun Song, Chieun Hwang, Jung Eun Lee, Yeon-Hee Lim, Chae Oh |
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