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

机译:犬基质金属蛋白酶-2(MMP-2)的分离与鉴定

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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.
机译:由成纤维细胞,软骨细胞和骨髓单核细胞系产生的犬明胶酶在非还原酶谱中的表观分子量为62kDa。该酶具有与人基质金属蛋白酶(MMP)2相似的特性,并且在Western blotting分析中与针对人MMP-2的绵羊多克隆抗血清产生交叉反应。从细胞培养基中纯化出62kDa的犬蛋白,印迹到聚偏二氟乙烯(PVDF)膜上后确定N端氨基酸序列。该序列与人MMP-2公开的序列87%相同。因此,我们认为该酶是犬MMP-2。

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