36

Biochimica et Biophysics Acta, 528 (1978) 36-46 0 Elsevier/North-Holland Biomedical Press

BBA 57111 MONOACYLGLYCEROL HYDROLASE ACTIVITY SMALL INTESTINAL EPITHELIAL CELLS

OF ISOLATED

RAT

B.J.P. DE JONG and W.C. HULSMANN Department of Biochemistry P.O. Box 1738, Rotterdam

I, Faculty of Medicine, (The Netherlands)

Erasmus

University

Rotterdam,

(Received July 5th, 1977)

Summary 1. Albumin is the preferred stabilizer of the higher monoacylglycerol substrates, since the highest activity was measured with albumin rather than with Triton X-100 or other detergents tested. 2. The monoacylglycerol hydrolase activity may be strongly influenced by the amount of albumin used as the only emulsifier. Possible models for the physical states of the substrate are discussed. 3. The reaction rates with l- and 2-monoacylglycerols are generally similar, but may vary accbrding to the physical states of the substrates. 4. The same enzyme hydrolyzes both l- and 2-isomers since the hydrolytic activities were found to be competitive rather than additive. For both isomers identical apparent K, values