Purification and characterization of the human stromelysin catalytic domain expressed in Escherichia coli

Qizhuang Ye, Linda L. Johnson, Donald J. Hupe, Vijaykumar Baragi

Research output: Contribution to journalArticle

81 Citations (Scopus)

Abstract

Human stromelysin is a member of the matrix metalloproteinase family involved in connective tissue degradation. The stromelysin catalytic domain (SCD) lacking both propeptide and C-terminal fragment was expressed in Escherichia coli in soluble and insoluble forms. The insoluble SCD was refolded to the active form in high yield. The protein showed remarkable thermal stability and was able to cleave a thiopeptolide substrate and its natural substrate proteoglycan. The stable and active 20-kDa protein provides an opportunity to elucidate the structure as well as the mechanism of catalysis and inhibition for matrix metalloproteinases.

Original languageEnglish (US)
Pages (from-to)11231-11235
Number of pages5
JournalBiochemistry
Volume31
Issue number45
StatePublished - 1992
Externally publishedYes

Fingerprint

Matrix Metalloproteinase 3
Escherichia coli
Purification
Catalytic Domain
Matrix Metalloproteinases
Proteoglycans
Substrates
Catalysis
Connective Tissue
Proteins
Thermodynamic stability
Hot Temperature
Tissue
Degradation

ASJC Scopus subject areas

  • Biochemistry

Cite this

Purification and characterization of the human stromelysin catalytic domain expressed in Escherichia coli. / Ye, Qizhuang; Johnson, Linda L.; Hupe, Donald J.; Baragi, Vijaykumar.

In: Biochemistry, Vol. 31, No. 45, 1992, p. 11231-11235.

Research output: Contribution to journalArticle

Ye, Qizhuang ; Johnson, Linda L. ; Hupe, Donald J. ; Baragi, Vijaykumar. / Purification and characterization of the human stromelysin catalytic domain expressed in Escherichia coli. In: Biochemistry. 1992 ; Vol. 31, No. 45. pp. 11231-11235.
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