A mass spectrometric study of the structure of sterol carrier protein SCP2 from rat liver.
The amino acid sequence of Sterol Carrier Protein2 (SCP2) isolated from rat has been investigated. Using a novel mass spectrometric mapping approach, the C-terminus was found to be extended beyond the previously published sequence. Carbohydrate analysis of SCP2 samples suggest the presence of tightly bound mannose oligosaccharide of 5-10 residues, although probably not in a glycoprotein linkage.
Morris
H R
HR
Medical Products Department, E.I. du Pont de Nemours & Company, Wilmington, DE 19898.
Larsen
B S
BS
Billheimer
J T
JT
D000595:Amino Acid Sequence; D000818:Animals; D002352:Carrier Proteins / Q000302:isolation & purification*; D003488:Cyanogen Bromide; D008099:Liver / Q000378:metabolism*; D013058:Mass Spectrometry; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000032:analysis; D010940:Plant Proteins; D051381:Rats; D013261:Sterols / Q000378:metabolism*; D014357:Trypsin
D002352:Carrier Proteins; D010446:Peptide Fragments; D010940:Plant Proteins; D013261:Sterols; C072087:sterol carrier proteins; D014357:Trypsin; D003488:Cyanogen Bromide