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...

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Veröffentlicht in:	Journal of natural products (Washington, D.C.) D.C.), 1990-07, Vol.53 (4), p.867-874
Hauptverfasser:	Beutler, John A, Alvarado, Ada Belinda, Schaufelberger, Daniel E, Andrews, Pamela, McCloud, Thomas G
Format:	Artikel
Sprache:	eng
Schlagworte:	560300 - Chemicals Metabolism & Toxicology Binding, Competitive BIOCHEMICAL REACTION KINETICS Biological and medical sciences Biological Factors - analysis Caenorhabditis elegans Proteins CARCINOGENS Carrier Proteins Chemical Fractionation CHROMATOGRAPHY Chromatography, High Pressure Liquid Cyanobacteria - analysis ESTERS FRACTIONATION General pharmacology KINETICS LIQUID COLUMN CHROMATOGRAPHY Medical sciences MEMBRANE PROTEINS METABOLISM Methods ORGANIC COMPOUNDS Pharmacognosy. Homeopathy. Health food Pharmacology. Drug treatments PHORBOL ESTERS PLANTS Plants - analysis Protein Kinase C PROTEINS RADIATION, THERMAL, AND OTHER ENVIRON. POLLUTANT EFFECTS ON LIVING ORGS. AND BIOL. MAT REACTION KINETICS RECEPTORS Receptors, Drug - metabolism SEPARATION PROCESSES Ultraviolet Rays
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Zusammenfassung:	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.
ISSN:	0163-3864 1520-6025
DOI:	10.1021/np50070a014