Purification of insect vitellogenin and vitellin by gel-immobilized ferric chelate.
Vitellogenin and vitellin of Manduca sexta and some other insect species were purified by immobilized metal ion affinity chromatography. Ferric ion was chosen as the immobilized metal ion. Agarose-bound carboxymethylpicolylamine was used as the chelating adsorbent for the ferric ion. Vitellogenin and vitellin, both phosphorylated lipoproteins, were shown to bind specifically to the iron. The general applicability of immobilized ferric ion affinity chromatography for the purification of insect vitellogenin and vitellin is suggested.
van Heusden
M C
MC
Department of Biochemistry, Biological Sciences West, University of Arizona, Tucson 85721.
Fogarty
S
S
Porath
J
J
Law
J H
JH
D000818:Animals; D002846:Chromatography, Affinity / Q000379:methods*; D004527:Egg Proteins / Q000737:chemistry / Q000302:isolation & purification*; D005260:Female; D006458:Hemolymph / Q000737:chemistry; D007313:Insecta / Q000737:chemistry*; D007502:Iron Chelating Agents; D009036:Moths / Q000737:chemistry; D010766:Phosphorylation; D014819:Vitellogenins / Q000737:chemistry / Q000302:isolation & purification*
D004527:Egg Proteins; D007502:Iron Chelating Agents; D014819:Vitellogenins