Purification and characterization of sn-1-stearoyl-2-arachidonoylglycerol kinase from pig testes.
1-Stearoyl-2-arachidonoylglycerol (SAG) kinase was identified in the particulate fraction of pig testes. This activity was enriched by hydroxyapatite and blue dye chromatography. The enzyme was selective for polyunsaturated diradylglycerol species and activity was not modulated by other diradylglycerol species or sphingomyelin metabolites. Further purification resulted in the isolation of 55 and 50 kDa proteins that corresponded with SAG kinase activity. These results support the view that the phosphorylation of polyunsaturated diradylglycerol is regulated by structural determinants in the molecule.
Hodgkin
M N
MN
Institute for Cancer Studies, The Medical School, University of Birmingham, Edgbaston, U.K.
Gardner
S D
SD
Rose
S
S
Paterson
A
A
Martin
A
A
Wakelam
M J
MJ
D000818:Animals; D002855:Chromatography, Thin Layer; D004075:Diglycerides / Q000378:metabolism* / Q000494:pharmacology; D008297:Male; D010766:Phosphorylation; D017853:Phosphotransferases (Alcohol Group Acceptor) / Q000187:drug effects / Q000302:isolation & purification* / Q000378:metabolism; D016622:Silver Staining; D013347:Subcellular Fractions / Q000201:enzymology; D013379:Substrate Specificity; D013552:Swine; D013737:Testis / Q000201:enzymology*
D004075:Diglycerides; C075809:1-stearoyl-2-arachidonoylglycerol; C104998:1-stearoyl-2-arachidonoylglycerol kinase; D017853:Phosphotransferases (Alcohol Group Acceptor); C013965:diolein