acid-hydrolysing lysophospholipase from rat brain
نویسنده
چکیده
A lysosophosphatidic acid (LPA)-hydrolysing lysophospholipase was purified from rat brain and characterized. This membranebound lysophospholipase was solubilized by using n-octyl glucoside and purified by sequential cation, hydrophobic and gel-filtration chromatography. The purified protein has a mass of 80 kDa as assayed by SDS/PAGE. This lysophospholipase catalysed the hydrolysis of a variety of lysophosphatidic acids, but with different rates, depending on the length and degree of saturation of the sn-I acyl group (1-oleoyl-LPA 1-stearoyl-
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تاریخ انتشار 2005