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One-step immunoaffinity purification and partial characterisation of a growth hormone from the pituitary gland of the African catfish, <i>Clarias gariepinus</i> (Burchell), <b><i>in</i></b>: <i>Seventh forum for applied biotechnology, PAND, Gent 30 September - October 1993, abstracts.</i> pp. 57","BEntID":39344,"PublicFlag":1,"CheckedFlag":0,"wosflag":0,"vabbflag":0,"RefStringPartII":", <b><i>in</i></b>: <i>Seventh forum for applied biotechnology, PAND, Gent 30 September - October 1993, abstracts.</i> pp. 57","DocTypID":17,"DocType":"Book chapters","MarineFlag":0,"FreshFlag":1,"BrackishFlag":0,"TerrestrialFlag":0,"Authorstring":"Lescroart, O.; Berghman, L.R.; Roelants, I.; Ollevier, F.P.; Kuhn, E.; Van Leuven, F.; Vandesande, F.","OrigTitleTranslFlag":0,"Authorstringtrunc":"Lescroart, O. <i>et al.</i>","Englishabstract":"Growth hormone (GH) wa8 purified from African catfish (<i>Clarias gariepinus</i>) pituitary extracts in a single step, using immuno-affinity chromatography. An anti-chicken GH monoclonal antibody, specifically cross-reacting with the African catfish hypophyseal somatotropes, was coupled to CNBr-activated Sepharose (5mg IgG/ml gel). Crude pituitary extracts were run as such over the immunoadsorbent. Although reversed-phase HPLC analysis of the eluted material showed two partially matching peaks, subsequent SDS-PAGE showed one single band upon silver staining. The apparent molecular weight of the purified molecule (as assessed by SDS-PAGE) was approximately 23,000 Da. The amino terminal end of the protein was homogenous and with the exception of 1 substitution at position 3, the first 30 residus matched the proposed protein sequence for GH of the channel catfish (<i>Ictalurus punctatus</i>). 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