Complete amino-acid sequence of the naturally occurring A2 activator protein for enzymic sphingomyelin degradation: identity to the sulfatide activator protein (SAP-1).
The naturally occurring A2 activator protein for enzymic sphingolipid degradation is characterized by complete amino-acid sequence and carbohydrate content. It consists of 79 amino-acid residues and has a molecular mass of 8.875 kDa. The polypeptide chain contains 2 mol of N-acetylglucosamine, bound to asparagine in position 21, as well as 2 mol of galactose and mannose per mol protein. The primary structure of the A2 activator protein is identical to that of the sulfatide activator protein (SAP-1). Possible differences in the carbohydrate content are discussed.
Kleinschmidt
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T
Max-Planck-Institut für Biochemie, Martinsried bei München.
Christomanou
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H
Braunitzer
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G
D000595:Amino Acid Sequence; D002851:Chromatography, High Pressure Liquid; D005260:Female; D005776:Gaucher Disease / Q000378:metabolism*; D006023:Glycoproteins / Q000302:isolation & purification; D006801:Humans; D008875:Middle Aged; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000302:isolation & purification; D049231:Saposins; D049128:Sphingolipid Activator Proteins; D013154:Spleen / Q000032:analysis; D014357:Trypsin
D006023:Glycoproteins; C483345:PSAP protein, human; D010446:Peptide Fragments; D049231:Saposins; D049128:Sphingolipid Activator Proteins; D014357:Trypsin