Purification of progelatinase A (matrix metalloproteinase 2) and a tissue inhibitor of metalloproteinase-2 (TIMP-2) from T98G human glioblastoma cells

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Title
Purification of progelatinase A (matrix metalloproteinase 2) and a tissue inhibitor of metalloproteinase-2 (TIMP-2) from T98G human glioblastoma cells
Author(s)
Ho Jae Lee; Myung Chul Chung; Choong Hwan Lee; Hyo Kon Chun; Yung Hee Kho
Bibliographic Citation
BMB Reports, vol. 28, no. 1, pp. 33-39
Publication Year
1995
Abstract
The Gelatinases (typeIV collagenases) are metalloproteinases that may play an important role in tumor invasion and metastasis. Progelatinase A was purified from a conditioned medium of T98G human glioblastoma cells. TIMP-2 complexed progelatinase A and free progelatinase A were separated by heparin affinity HPLC. The final product was homogeneous on SDS-PAGE, with a molecular weight of 64,000 daltons without reduction. TIMP-2 and free progelatinase A were separated from TIMP-2 complexed progelatinase A by reverse-phase HPLC in the presence of trifluoroacetic acid. TIMP-2 complexed progelatinase A was resistant to activation by p-aminophenyl mercuric acetate (APMA), and showed less than 20% of the activity of the TIMP-2 free active enzyme. TIMP-2 free progelatinase A was easily activated to the mature form with a molecular weight of 57,000 daltons by APMA and showed high activity compared to the TIMP-2 complexed enzyme.
Keyword
Matrix metalloproteinasesTIMPglioblastoma
ISSN
1225-8687
Publisher
Korea Soc-Assoc-Inst
Type
Article
Appears in Collections:
Division of Bio Technology Innovation > SME Support Center > 1. Journal Articles
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