Separation of insect hemolymph proteins by cascade‐mode multiaffinity chromatography

Publisher Website
Google Scholar
Abstract
The hemolymph of the adult female Manduca sexta was fractionated by cascade-mode multiaffinity chromatography (CASMAC) on a main-line tandem column chain containing Zn2+-TED, T-gel, Ni2+-DPA, and phenylsepharose and a side-line column containing Zn2+-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.