N-terminal amino-acid sequence of a sphingolipid activator protein missing in a new human Gaucher disease variant.
A naturally occurring non-enzymic sphingolipid activator protein (A1a activator) shown previously to be immunochemically not detectable in a new variant of human Gaucher disease (glucosylceramide-lipidosis) without glucosylceramidase deficiency was characterized by partial sequence analysis. The N-terminal amino-acid sequence of the A1a activator--a glycoprotein with high carbohydrate content--could be determined up to position 38. About 20% of the polypeptide chain are shorter by two amino-acid residues at the N-terminal end. Position 22 seems to be occupied by a carbohydrate-binding asparagine. The N-terminus of the A1a activator does not show any homology with the activator for the enzymic sulfatide degradation.
Christomanou
H
H
Max-Planck-Institut für Psychiatrie, München.
Kleinschmidt
T
T
Braunitzer
G
G
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D005260:Female; D005776:Gaucher Disease / Q000378:metabolism*; D006023:Glycoproteins / Q000302:isolation & purification; D006801:Humans; D008875:Middle Aged; D008969:Molecular Sequence Data; D049231:Saposins; D049128:Sphingolipid Activator Proteins; D013154:Spleen / Q000032:analysis
D000596:Amino Acids; D006023:Glycoproteins; C483345:PSAP protein, human; D049231:Saposins; D049128:Sphingolipid Activator Proteins