
doi: 10.1007/bf02531961
pmid: 4343497
Abstract1‐Acyl‐lysolecithin acyltransferase has been demonstrated in the microsomal fraction of hamster intestinal mucosa. The characteristics of the enzyme, with respect to substrate concentration, time of incubation and protein concentration, were studied. Ca++ was found to severely inhibit enzymatic activity. More modest inhibitors were found to be Mg++ and F−; EDTA and albumin had no effect. Enzyme activity was reduced when palmityl CoA was substituted for oleoyl CoA as substrate. The specific activity of intestinal microsomes was modestly greater than liver microsomes.
Male, Carbon Isotopes, Chromatography, Lysophosphatidylcholines, Silicon Dioxide, Egg Yolk, Fluorides, Phospholipases, Albumins, Cricetinae, Microsomes, Phosphatidylcholines, Animals, Calcium, Female, Magnesium, Chromatography, Thin Layer, Intestinal Mucosa, Acyltransferases, Edetic Acid
Male, Carbon Isotopes, Chromatography, Lysophosphatidylcholines, Silicon Dioxide, Egg Yolk, Fluorides, Phospholipases, Albumins, Cricetinae, Microsomes, Phosphatidylcholines, Animals, Calcium, Female, Magnesium, Chromatography, Thin Layer, Intestinal Mucosa, Acyltransferases, Edetic Acid
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