Partial sequencing of two forms of concanavalin A-unbound collagenase inhibitor from bovine gingiva

Arch Oral Biol. 1993 Oct;38(10):917-8. doi: 10.1016/0003-9969(93)90102-r.

Abstract

Three forms of collagenase inhibitor, one ConA-bound and two ConA-unbound, were extensively purified from bovine gingiva by sequential column chromatography. Analysis by sodium dodecyl sulphate-polyacrylamide gel electrophoresis revealed that inhibitory activity resides in proteins with M(r) of 26000-28000 and 22000 for ConA-bound and two ConA-unbound inhibitors, respectively. Of these, two ConA-unbound inhibitors were partially sequenced in the first 12 amino acids and found to have an identical sequence. The NH2-terminal sequence had 100% identity with TIMP-2 or MI.

MeSH terms

  • Amino Acid Sequence*
  • Animals
  • Cattle
  • Chromatography, Agarose
  • Chromatography, Ion Exchange
  • Collagenases / analysis*
  • Concanavalin A / chemistry*
  • Electrophoresis, Polyacrylamide Gel
  • Gingiva / chemistry*
  • Gingiva / enzymology*
  • Glycoproteins / analysis*
  • Matrix Metalloproteinase Inhibitors*
  • Metalloendopeptidases / analysis*
  • Molecular Sequence Data
  • Sodium Dodecyl Sulfate
  • Tissue Inhibitor of Metalloproteinases

Substances

  • Glycoproteins
  • Matrix Metalloproteinase Inhibitors
  • Tissue Inhibitor of Metalloproteinases
  • Concanavalin A
  • Sodium Dodecyl Sulfate
  • Collagenases
  • Metalloendopeptidases