SINGLE-STEP IMMUNOAFFINITY PURIFICATION OF THE NEUROPEPTIDE SERICOTROPIN USING POLYCLONAL ANTIBODIES TOWARDS THE SYNTHETIC N-TERMINAL FRAGMENT OF THE MOLECULE
D. Kodrik et al., SINGLE-STEP IMMUNOAFFINITY PURIFICATION OF THE NEUROPEPTIDE SERICOTROPIN USING POLYCLONAL ANTIBODIES TOWARDS THE SYNTHETIC N-TERMINAL FRAGMENT OF THE MOLECULE, European journal of entomology, 94(2), 1997, pp. 307-309
An immunoaffinity chromatography of the neuropeptide sericotropin usin
g rabbit polyclonal antibodies towards the 16 amino acids synthetic fr
agment of the molecule was used for the purification of the peptide fr
om Galleria mellonella larval brains. The method employed CNBr-activat
ed Sepharose and the isolated IgG fraction of the corresponding antise
rum. The purity of the peptide was proven by means of HPLC and immunob
lotting techniques.