Palmitoyl CoA ligase activity in hepatopancreas and gill microsomes of the fresh water shrimp Macrobrachium borellii

GONZALEZ BARO, M.R.; IRAZU, C.E.; POLLERO, R.J.

COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY. PART B, BIOCHEMISTRY & MOLECULAR BIOLOGY.

ELSEVIER SCIENCE INC

Lugar: Amsterdam; Año: 1990 vol. 97B p. 129 - 133

1096-4959

1. The kinetic parameters of microsomal palmitoyl-CoA ligase from gills and hepatopancreas of Macrobrachium borellii were investigated.2. The optimal temperature for the enzymatic activity was 37°C in gill microsomes and 30°C in hepatopancreas microsomes.3. The maximal affinity of the enzyme for its substrate was higher in gill microsomes (apparent K m = 12.59 uM) compared with hepatopancreas microsomes (apparent Km= 49.74 uM).4. A lower lipid mobility in gill microsomes than in hepatopancreas microsomes was found. It was attributed to a high phosphatidyl ethanolamine content in gill membranes. This could also explain the differences in the optimal temperatures for the activities of the enzyme from both organs.