Data in support of the negative influence of divalent cations on (−)-epigallocatechin-3-gallate (EGCG)-mediated inhibition of matrix metalloproteinase-2 (MMP-2)
In this data article we have provided evidence for the negative influence of divalent cations on (−)‐epigallocatechin-3-gallate (EGCG)-mediated inhibition of matrix metalloproteinase-2 (MMP-2) activity in cell-free experiments. Chelating agents, such as EDTA and sodium citrate alone, did not affect...
| Main Authors: | , , |
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| Format: | Article |
| Language: | English |
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Elsevier
2016-03-01
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| Series: | Data in Brief |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S2352340915003947 |
| _version_ | 1831689197752156160 |
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| author | Gauri Deb Sahil Batra Anil M. Limaye |
| author_facet | Gauri Deb Sahil Batra Anil M. Limaye |
| author_sort | Gauri Deb |
| collection | DOAJ |
| description | In this data article we have provided evidence for the negative influence of divalent cations on (−)‐epigallocatechin-3-gallate (EGCG)-mediated inhibition of matrix metalloproteinase-2 (MMP-2) activity in cell-free experiments. Chelating agents, such as EDTA and sodium citrate alone, did not affect MMP-2 activity. While EDTA enhanced, excess of divalent cations interfered with EGCG-mediated inhibition of MMP-2. |
| first_indexed | 2024-12-20T10:44:59Z |
| format | Article |
| id | doaj.art-af6f52433b664f51909bef3eb6d07508 |
| institution | Directory Open Access Journal |
| issn | 2352-3409 |
| language | English |
| last_indexed | 2024-12-20T10:44:59Z |
| publishDate | 2016-03-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Data in Brief |
| spelling | doaj.art-af6f52433b664f51909bef3eb6d075082022-12-21T19:43:26ZengElsevierData in Brief2352-34092016-03-016461465Data in support of the negative influence of divalent cations on (−)-epigallocatechin-3-gallate (EGCG)-mediated inhibition of matrix metalloproteinase-2 (MMP-2)Gauri Deb0Sahil Batra1Anil M. Limaye2Department of Biosciences and Bioengineering, Indian Institute of Technology Guwahati, Guwahati 781039, Assam, IndiaDepartment of Biosciences and Bioengineering, Indian Institute of Technology Guwahati, Guwahati 781039, Assam, IndiaCorresponding author.; Department of Biosciences and Bioengineering, Indian Institute of Technology Guwahati, Guwahati 781039, Assam, IndiaIn this data article we have provided evidence for the negative influence of divalent cations on (−)‐epigallocatechin-3-gallate (EGCG)-mediated inhibition of matrix metalloproteinase-2 (MMP-2) activity in cell-free experiments. Chelating agents, such as EDTA and sodium citrate alone, did not affect MMP-2 activity. While EDTA enhanced, excess of divalent cations interfered with EGCG-mediated inhibition of MMP-2.http://www.sciencedirect.com/science/article/pii/S2352340915003947 |
| spellingShingle | Gauri Deb Sahil Batra Anil M. Limaye Data in support of the negative influence of divalent cations on (−)-epigallocatechin-3-gallate (EGCG)-mediated inhibition of matrix metalloproteinase-2 (MMP-2) Data in Brief |
| title | Data in support of the negative influence of divalent cations on (−)-epigallocatechin-3-gallate (EGCG)-mediated inhibition of matrix metalloproteinase-2 (MMP-2) |
| title_full | Data in support of the negative influence of divalent cations on (−)-epigallocatechin-3-gallate (EGCG)-mediated inhibition of matrix metalloproteinase-2 (MMP-2) |
| title_fullStr | Data in support of the negative influence of divalent cations on (−)-epigallocatechin-3-gallate (EGCG)-mediated inhibition of matrix metalloproteinase-2 (MMP-2) |
| title_full_unstemmed | Data in support of the negative influence of divalent cations on (−)-epigallocatechin-3-gallate (EGCG)-mediated inhibition of matrix metalloproteinase-2 (MMP-2) |
| title_short | Data in support of the negative influence of divalent cations on (−)-epigallocatechin-3-gallate (EGCG)-mediated inhibition of matrix metalloproteinase-2 (MMP-2) |
| title_sort | data in support of the negative influence of divalent cations on epigallocatechin 3 gallate egcg mediated inhibition of matrix metalloproteinase 2 mmp 2 |
| url | http://www.sciencedirect.com/science/article/pii/S2352340915003947 |
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