A single-center experience of detecting coronary anomalies on 64-slice computed tomography.

Background: The detection of coronary anomalies is of major clinical significance. Coronary anomalies have been identified as a frequent cause of sudden death, particularly in young athletes. Multiple series have successfully demonstrated the ability of 64-slice computed tomography (CT) to identify coronary anomalies.

Hydrophobic nature of mammalian ceramide glycanases: purified from rabbit and rat mammary tissues.

The ceramide glycanase (CGase) activities, which cleave the intact oligosaccharide chain and the ceramide moiety of a glycosphingolipid, have been characterized from two mammalian sources. The enzymatic activities are almost comparable in rabbit and rat mammary tissues. The majority of the activities has been concentrated in the soluble fraction which could be partially purified using hydrophobic columns.

Ceramide glycanase from rat mammary tissues: inhibition by PPMP(D-/L-) and its probable role in signal transduction.

A ceramide glycanase (CGase activity has been characterized from lactating rat mammary tissue which cleaves the glycosidic bond between sphingosine and the glucose chain of a glycosphingolipid (GSL) thus liberating the intact oligosaccharide chain from a GSL. The majority (65%) of the hydrolase activity was detected in the supernatant fraction when the rat mammary tissue homogenate was centrifuged at 100,000 x g. Attempts to purify the enzyme indicated that the CGase protein is of hydrophobic nature as it binds to hydrophobic columns.