Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.4.21.1 (chymotrypsin)
 10,938 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Saposin B is involved in the hydrolysis of sulfatides, GM1 ganglioside, globotriaosylceramide, and several other sphingolipids and glycerolipids by lysosomal hydrolases. Saposin B is one of four small glycoproteins (saposins) derived from prosaposin. The carbohydrate chain of saposin B was removed and deglycosylated saposin B was characterized and compared with native saposin B. Deglycosylated saposin B stimulated the enzymatic hydrolysis of ganglioside GM1 by acid beta-galactosidase and sulfatide by arylsulfatase A to the same extent as native saposin B. In addition deglycosylated saposin B bound sulfatide and GM1 ganglioside identical to native saposin B. The stability of native saposin B to proteolytic digestion was unchanged by deglycosylation. Neither native saposin B nor deglycosylated saposin B were hydrolyzed by trypsin, endoproteinase Glu-C (V-8), chymotrypsin, or a mixture of acid proteases isolated from human testis. Unlike its effect on metabolic stability, the carbohydrate chain appears to affect folding of saposin B. When native and deglycosylated saposin B were reduced under denaturing conditions and refolded under identical conditions examination of the refolded products indicated that each protein was refolded in a qualitatively different way. A human mutation in saposin B-deficient metachromatic leukodystrophy, in which its glycosylation site is eliminated, has been reported. Our observations suggest that instability of the mutated saposin B is not due to the absence of a protective effect of the carbohydrate chain on proteolysis, but is likely due to aberrant folding resulting from the absence of a carbohydrate chain.
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PMID:The effect of carbohydrate removal on stability and activity of saposin B. 809 82

Synaptosomes incorporated mixed brain gangliosides at a rapid initial rate followed by a slower phase of net movement from the protein-associated fraction into the membrane core. The pattern of incorporated gangliosides reflected the pattern available for incorporation. Intact synaptosomes incorporated approximately 100 pmol GM1/mg protein. Synaptosomes preincubated with proteolytic enzymes (trypsin, chymotrypsin, and papain) at different pH values (6.2, 7.4, 7.8) incorporated more exogenous gangliosides than synaptosomes preincubated in buffer alone. This effect was maximal at pH 7.8, though analysis of variance revealed that the proteolytic treatment and pH effects were probably independent processes. Overall uptake of exogenous gangliosides correlated significantly with amount of membrane protein loss, indicating that initial access of exogenous gangliosides to synaptosomal membranes is retarded by cell-surface proteins. These results suggest synaptosomes as a useful alternative to cultured cells for investigating the interaction of gangliosides with other cell surface constituents.
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PMID:Uptake of exogenous gangliosides by rat brain synaptosomes. 982 Nov 55