Effect of phospholipids on alpha-1,2-mannosidase activity.
作者： W T Forsee , J D Springfield , J S Schutzbach
DOI: 10.1016/S0021-9258(18)33971-1
关键词: Microsome 、 Composition (visual arts) 、 Phospholipid 、 Membrane 、 Enzyme 、 Titration 、 Degree of unsaturation 、 Biochemistry 、 Micelle 、 Chemistry
摘要: Abstract An alpha-1,2-mannosidase has been solubilized and partially purified from rabbit liver microsomes (Forsee, W. T., Schutzbach, J. S. (1981) Biol. Chem. 256, 6577-6582). The enzyme was activated by the addition of zwitterionic phospholipids but maximal activity found to be relatively independent acyl chain length or degree unsaturation. Titration with increasing concentrations water-soluble long demonstrated that an ordered lipid structure either micelles bilayers required for alpha-mannosidase activity. Mixed Triton X-100 also enzyme. concentration phospholipid in mixed activation dependent upon length, unaffected this parameter. negatively charged not only failed activate inhibited presence phospholipids. Inhibition pH inhibition at values 6.0 lower. These results suggest could subject modulation composition microsomal membranes.
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