Dereplication of phorbol bioactives: Lyngbya majuscula and Croton cuneatus.
Lyngbya majuscula and Croton cuneatus were used as prototypes for the dereplication of phorbol ester receptor binding activity using a combination of hplc-uv and online phorbol dibutyrate (PDBu) receptor binding and batch fractionation over either Si gel or diolbonded Si gel. Debromoaplysiatoxin was responsible for the bioactivity of Lyngbya, whereas a complex of potent phorbol esters was detected in C. cuneatus.
Beutler
J A
JA
PRI/DynCorp
Alvarado
A B
AB
Schaufelberger
D E
DE
Andrews
P
P
McCloud
T G
TG
D001667:Binding, Competitive; D001685:Biological Factors / Q000032:analysis*; D029742:Caenorhabditis elegans Proteins; D002352:Carrier Proteins; D005591:Chemical Fractionation; D002851:Chromatography, High Pressure Liquid; D000458:Cyanobacteria / Q000032:analysis*; D008722:Methods; D010944:Plants / Q000032:analysis*; D011493:Protein Kinase C; D011955:Receptors, Drug / Q000378:metabolism*; D014466:Ultraviolet Rays
D001685:Biological Factors; D029742:Caenorhabditis elegans Proteins; D002352:Carrier Proteins; D011955:Receptors, Drug; C083141:phorbol ester binding protein; C027776:phorbol ester receptor; D011493:Protein Kinase C