Isolation and identification of canine matrix metalloproteinase-2 (MMP-2)

被引:26
作者
Coughlan, AR
Robertson, DHL
Burke, R
Beynon, RJ
Carter, SD
机构
[1] Univ Liverpool, Dept Vet Pathol, Liverpool L69 3BX, Merseyside, England
[2] Univ Liverpool, Dept Vet Clin Sci & Anim Husb, Liverpool L69 3BX, Merseyside, England
[3] Univ Manchester, Inst Sci & Technol, Dept Biochem & Appl Mol Biol, Manchester M60 1QD, Lancs, England
基金
英国惠康基金;
关键词
MMP; gelatinase; dog; purification; sequencing;
D O I
10.1016/S1090-0233(05)80016-4
中图分类号
S85 [动物医学(兽医学)];
学科分类号
0906 ;
摘要
A canine gelatinase, with an apparent molecular mass of 62kDa 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 62kDa 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.
引用
收藏
页码:231 / 237
页数:7
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