Cockle S M, Smyth D G
Biosci Rep. 1986 Jun;6(6):519-26. doi: 10.1007/BF01114948.
An antibody was raised to the synthetic pentapeptide pGluHisProGlyLys which, in radioimmunoassay (RIA), could detect the pentapeptide at a level of 10 fmole per tube and exhibited less than 0.5 per cent cross reactivity with a series of related peptides. The RIA was used to demonstrate the presence of C-terminally extended forms of thyrotropin releasing hormone (TRH) in rat hypothalamus. After extraction, the endogenous peptides were resolved by gel exclusion chromatography and TRH-extended peptides were revealed by trypsin digestion to release the pentapeptide. The TRH extended peptides occurred in substantial quantity, approximately 11 pmoles/g, indicating that only partial processing of the gene duplicated prohormone takes place.
针对合成五肽pGluHisProGlyLys制备了一种抗体，该抗体在放射免疫测定（RIA）中能够检测到每管10飞摩尔水平的五肽，并且与一系列相关肽的交叉反应率低于0.5%。该RIA用于证明大鼠下丘脑促甲状腺激素释放激素（TRH）C末端延伸形式的存在。提取后，内源性肽通过凝胶排阻色谱法分离，TRH延伸肽通过胰蛋白酶消化释放五肽来揭示。TRH延伸肽大量存在，约为11皮摩尔/克，表明基因重复前体激素仅发生部分加工。
