Separation of insect hemolymph proteins by cascade-mode multi-affinity chromatography.
The hemolymph of the adult female Manduca sexta was fractionated by cascade-mode multi-affinity chromatography (CASMAC) on a main-line tandem column chain containing Zn(2+)-TED, T-gel, Ni(2+)-DPA, and phenylsepharose and a side-line column containing Zn(2+)-DPA. The technique separated some of the previously described major hemolymph proteins, and yielded a number of fractions with simple composition. Some of these fractions contained only less abundant proteins of Manduca hemolymph. Thus, it appears that CASMAC would be a very useful fractionation technique for purification and characterization of the minor proteins of insect hemolymph.
Samaraweera
P
P
Center for Insect Science, University of Arizona, Tucson 85721.
Porath
J
J
Law
J H
JH
D000818:Animals; D002846:Chromatography, Affinity / Q000379:methods*; D006458:Hemolymph / Q000737:chemistry*; D009036:Moths / Q000737:chemistry*; D011506:Proteins / Q000302:isolation & purification*
D011506:Proteins