作者: P Bacha , J R Murphy , S Reichlin
DOI: 10.1016/S0021-9258(18)33021-7
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摘要: Abstract We have separately coupled a modified thyrotropin-releasing hormone (TRH) molecule to two diphtheria toxin-related polypeptides, CRM26 and CRM45. Both polypeptides are enzymatically active but only CRM45 contains the hydrophobic domain of toxin molecule. The TRH-CRM45 conjugate caused 50% inhibition protein synthesis in GH3 rat pituitary cells at 3 X 10(-9) M. alone was 200 500 times less toxic than conjugate. Intoxication by prevented excess TRH, preincubation with antitoxin, or reduction disulfide cross-link. In addition, no more itself 3T3 which lack TRH receptors. contrast, TRH-CRM26, although it retained enzymatic activity, nontoxic for even 10(-7) Binding experiments showed that both conjugates compete receptors comparable affinities. potential role entry is discussed.