Method For Isolation Of Mmp-7-Ase Isoenzymes From Rat Muscle Tissue Extract

Janos G. Guoth, Istvan Sohar, Marta Zarandi, Tamas Janaky

Research output: Contribution to journalArticle

2 Citations (Scopus)


Two MMP-7-ase isoenzymes were purified 100-fold from rat muscle extract to apparent homogeneity, with an overall yield of 10%, using homogenization, ultracentrifugation, high-performance aqueous size-exclusion and high-performance anion exchange chromatography methods. When using a TSK G-2000SW column, the separation resulted in a 6-fold purification and 30% recovery of isoenzymes B and C. This concentrated enzyme extract was then passed through a TSK-DEAE-2SW column, using salt gradient at pH 7.5, with an additional 25-fold purification and 90% recovery of the isoenzymes. Two symmetrical enzyme peaks, representing isoenzymes B and C, were detected when performing purity tests of the active enzymes on the anion exchanger and reversed-phase HPLC columns. The procedures involved are extraction, ultracentrifugation, chromatographies and enzyme assays and require less than five hours.

Original languageEnglish
Pages (from-to)361-374
Number of pages14
JournalPreparative Biochemistry
Issue number3
Publication statusPublished - Sep 1 1988

ASJC Scopus subject areas

  • Biochemistry
  • Genetics

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