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Comparative Study Of Lipoprotein Lipase In White And Brown Fat Of Rat (Rattus Norvegicus)
Published 1980 · Chemistry
Abstract 1. 1. More lipoprotein lipase of acetone ether powders of rat brown and epididymal fat is extracted by ammonium buffer than by NaCl barbital buffer. The presence of NaCl in the buffer determines great instability of the enzymatic preparation. 2. 2. The lipoprotein lipase of these two tissues have the same chromatographic behaviour on heparin-sepharose. Total purification is about 900 times. 3. 3. Purified enzymes are unstable. We have been able to show that NaCl is to a great extent responsible for this instability. 4. 4. Minimum molecular size is 64,000 for white fat lipoprotein lipase and 67,000 for brown fat lipoprotein lipase. 5. 5. The characteristics of the purified enzymes are identical and are comparable with those generally described.