Isolation and identification of canine matrix metalloproteinase-2 (MMP-2).
A canine gelatinase, with an apparent molecular mass of 62 kDa in non-reducing zymography, is produced by fibroblasts, chondrocytes and a myelomonocytic cell line. The enzyme has similar characteristics to human matrix metalloproteinase (MMP) 2 and cross-reacts in Western blotting analysis with a sheep polyclonal antiserum raised against human MMP-2. The 62 kDa canine protein was purified from cell culture media, and the N-terminal amino acid sequence determined following blotting on to a polyvinylidene difluoride (PVDF) membrane. The sequence was 87% identical to that published for human MMP-2. We therefore consider this enzyme to be canine MMP-2.
Coughlan
A R
AR
Department of Veterinary Pathology, University of Liverpool, UK.
Robertson
D H
DH
Burke
R
R
Beynon
R J
RJ
Carter
S D
SD
D000595:Amino Acid Sequence; D000818:Animals; D002478:Cells, Cultured; D004285:Dogs / Q000502:physiology*; D018093:Gelatinases / Q000737:chemistry / Q000302:isolation & purification*; D006801:Humans; D066298:In Vitro Techniques; D020778:Matrix Metalloproteinase 2; D008666:Metalloendopeptidases / Q000737:chemistry / Q000302:isolation & purification*; D008969:Molecular Sequence Data; D017386:Sequence Homology, Amino Acid
D018093:Gelatinases; D008666:Metalloendopeptidases; D020778:Matrix Metalloproteinase 2