The primary structure of a membrane-associated phospholipase A2 from human spleen.
The complete primary structure of membrane-associated phospholipase A2 purified from a human splenic membrane fraction was determined by sequence analysis of the peptides generated by lysyl endopeptidase and Staphylococcus aureus V8 protease cleavage. The enzyme consists of 124 amino acid residues corresponding to a molecular weight of 13,904. The primary structure reveals the characteristics of Group II phospholipases A2 and a large ratio of basic amino acid residues to acidic ones, that ratio being 3.4 : 1.
Kanda
A
A
Shionogi Research Laboratories, Shionogi & Co., Ltd., Osaka, Japan.
Ono
T
T
Yoshida
N
N
Tojo
H
H
Okamoto
M
M
D000595:Amino Acid Sequence; D002462:Cell Membrane / Q000201:enzymology; D002851:Chromatography, High Pressure Liquid; D006801:Humans; D008565:Membrane Proteins / Q000302:isolation & purification; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000032:analysis; D010740:Phospholipases / Q000302:isolation & purification*; D010741:Phospholipases A / Q000302:isolation & purification*; D054467:Phospholipases A2; D013154:Spleen / Q000201:enzymology*
D008565:Membrane Proteins; D010446:Peptide Fragments; D010740:Phospholipases; D010741:Phospholipases A; D054467:Phospholipases A2