Degradation of connective tissue proteins by serine proteases from Streptococcus pneumoniae

Harry Courtney

Research output: Contribution to journalArticle

8 Citations (Scopus)

Abstract

The proteolytic activity of pneumococcal culture supernatants was investigated. Phenylmethylsulfonyl fluoride and diisopropylfluorophosphate inhibited the proteolytic activity by 94% indicating that the enzymes are serine proteases. Zymogram analysis with inhibitors utilizing a non-denaturing gelatin substrate gel revealed two classes of serine proteases; one sensitive to calcium chelators and one resistant. Enzymes from the culture supernatant cleaved fibronectin, fibrinogen, elastin, and laminin; whereas bovine albumin, and the human immunoglobulins, IgG, IgM, and IgA, were not cleaved. These results indicate that pneumococci produce previously unrecognized serine proteases that degrade several tissue and blood proteins.

Original languageEnglish (US)
Pages (from-to)1023-1028
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume175
Issue number3
DOIs
StatePublished - Mar 29 1991

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Serine Proteases
Streptococcus pneumoniae
Connective Tissue
Tissue
Degradation
Phenylmethylsulfonyl Fluoride
Isoflurophate
Proteins
Elastin
Laminin
Enzymes
Gelatin
Fibronectins
Fibrinogen
Immunoglobulin A
Immunoglobulin M
Immunoglobulins
Blood Proteins
Albumins
Immunoglobulin G

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Degradation of connective tissue proteins by serine proteases from Streptococcus pneumoniae. / Courtney, Harry.

In: Biochemical and Biophysical Research Communications, Vol. 175, No. 3, 29.03.1991, p. 1023-1028.

Research output: Contribution to journalArticle

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