The presence of sphingomyelin-and ceramide-cleaving enzymes in the small intestinal tract
Å Nilsson - Biochimica et Biophysica Acta (BBA)-Lipids and Lipid …, 1969 - Elsevier
The crude protein fraction of human duodenal contents catalyzed the formation of ceramide
from sphingomyelin most efficiently at slightly alkaline pH in the presence of conjugated bile
salts. Under optimal conditions 1 ml duodenal contents hydrolyzed up to 300 nmole
sphingomyelin per h. The hydrolysis of ceramide to sphingosine and free fatty acids and the
reverse reaction were also catalyzed. The pH optimum of this reaction was about 7.6. That
the enzymes are of intestinal origin was indicated by the data obtained when sphingomyelin …
from sphingomyelin most efficiently at slightly alkaline pH in the presence of conjugated bile
salts. Under optimal conditions 1 ml duodenal contents hydrolyzed up to 300 nmole
sphingomyelin per h. The hydrolysis of ceramide to sphingosine and free fatty acids and the
reverse reaction were also catalyzed. The pH optimum of this reaction was about 7.6. That
the enzymes are of intestinal origin was indicated by the data obtained when sphingomyelin …
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