Partial sequencing of two forms of concanavalin A-unbound collagenase inhibitor from bovine gingiva.
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.
Mizuno
T
T
Department of Biochemistry, Niigata University School of Dentistry, Japan.
Igarashi
A
A
Nohara
H
H
D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D002847:Chromatography, Agarose; D002852:Chromatography, Ion Exchange; D017364:Collagenases / Q000032:analysis*; D003208:Concanavalin A / Q000737:chemistry*; D004591:Electrophoresis, Polyacrylamide Gel; D005881:Gingiva / Q000737:chemistry* / Q000201:enzymology*; D006023:Glycoproteins / Q000032:analysis*; D061965:Matrix Metalloproteinase Inhibitors; D008666:Metalloendopeptidases / Q000032:analysis*; D008969:Molecular Sequence Data; D012967:Sodium Dodecyl Sulfate; D019714:Tissue Inhibitor of Metalloproteinases
D006023:Glycoproteins; D061965:Matrix Metalloproteinase Inhibitors; D019714:Tissue Inhibitor of Metalloproteinases; D003208:Concanavalin A; D012967:Sodium Dodecyl Sulfate; D017364:Collagenases; D008666:Metalloendopeptidases