In a 1988 study conducted by Hugo Scheer and Harmut Kayser, biliproteins were extracted from the large white butterfly and puss moth and their respective properties were examined.  Their properties were compared to those of plant and algae biliproteins, and their distinguishing features were taken into account.
Unlile plant and algae biliproteins whose bilins are generally only derived from the IXα biliverdin isomer, the bilins of insect biliproteins are also derived from the IXγ isomer, which is almost exclusively found in Lepidoptera.  The study cited from M. Bois-Choussy and M. Barbier that these IXγ-series bile pigments are derived from cleavage of the porphyrin precursors at the C-15 (formerly γ) methine bridge, which is uncharacteristic of other mammalian and plant biliproteins. When the scientists examined biliproteins from both the large white butterfly and puss moth, they found that their polypeptides had a low α-helix content in comparison to phycobiliproteins.
It was hypothesised that the role of biliproteins in insects would also have a role related to light-absorption similar to that in plant and algae biliproteins. However, when the photochemical properties required for light-absorption were found absent in the biliprotein of the large white butterfly, this hypothesis was eliminated, followed by the assumption that those photochemical properties also do not occur in any other insect biliproteins.
Based on these examinations, it was concluded that insect biliproteins are only loosely related to those from plants and algae, due to the large number of differences they have regarding structure, chemical composition, derivation of bilins and general functions.