Properties of lipoprotein lipase extracted from livers of normal rats and livers and tumors of rats bearing Walker carcinosarcoma 256

• Published in: Archives of biochemistry and biophysics Vol. 98; no. 3; pp. 397 - 405
• Main Authors: Barclay, M., Garfinkel, E., Terebus-Kekish, O., Shah, E.B., deGuia, M., Barclay, R.K., Skipski, V.P.
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 01.09.1962
• Subjects: Animals; Carcinoma 256, Walker; Carcinosarcoma; Lipoprotein Lipase - chemistry; Liver - chemistry; Neoplasms; Neoplasms, Experimental; Old Medline; Rats; CARCINOSARCOMA/experimental; LIVER/chemistry; LIPOPROTEIN LIPASE/chemistry; NEOPLASMS/experimental
• ISSN: 0003-9861; 1096-0384
• DOI: 10.1016/0003-9861(62)90204-7

Extracts of acetone powders made from normal rat livers, and livers and tumor tissues from male rats bearing the Walker carcinosarcoma 256 have been made. No heparin was given to the animals at any time. The properties of the lipases studied indicate that they are lipoprotein lipases, even though they will hydrolyze well a 1.5% coconut oil emulsion. There is some indication that these enzymes preferentially hydrolyze the lower-density lipoproteins i.e., S f 100–400 and then proceed to the S f 20–100 and 0–20 classes, in in vitro experiments. The enzyme from the liver tissue of rats bearing the Walker carcinoma 256 is especially active in reducing the quantity of all the low-density lipoproteins measured in these experiments. The enzyme from tumor tissue is quite dependent upon heparin. The enzymes from all the tissues examined have characteristics which are like the lipoprotein lipase extracted from normal rat heart, and it may be suggested that the tissue extracts tested in these experiments do have lipoprotein lipase, or clearing factor, activities.