Rorstad O P
J Immunoassay. 1983;4(1):49-63. doi: 10.1080/15321818308056999.
The regions of the somatostatin (SRIF) molecule recognized by five antisera were systematically studied using three radioligands (125I-N-Tyr-SRIF, [125I-Tyr1]-SRIF and [125I-Tyr11]- SRIF) and SRIF analogs containing sequential substitutions with alanine or tyrosine. Antisera SA and moreso SB had N-terminal specificity when used with [125 I-Tyr11]-SRIF but central molecular specificity when studied with the two N-terminal radiolabelled analogs. The N-terminal and central specific populations of antibodies in antiserum SB were separable by immunoaffinity adsorption using immobilized [Tyr1]-SRIF. It is of practical significance that the same antiserum (SB) could be used with different radioligands to perform N-terminal and central specific radioimmunoassays (RIAs). The central specific RIA detected SRIF-14 and SRIF-28 on an approximately equimolar basis whereas the N-terminal specific RIA was selective for SRIF-14.
利用三种放射性配体（125I-N-酪氨酸-生长抑素（SRIF）、[125I-酪氨酸1]-SRIF和[125I-酪氨酸11]-SRIF）以及含有丙氨酸或酪氨酸顺序取代的SRIF类似物，系统研究了五种抗血清所识别的生长抑素（SRIF）分子区域。抗血清SA以及更明显的抗血清SB与[125I-酪氨酸11]-SRIF一起使用时具有N端特异性，但与两种N端放射性标记类似物一起研究时具有分子中央特异性。抗血清SB中抗体的N端和中央特异性群体可通过使用固定化的[酪氨酸1]-SRIF进行免疫亲和吸附来分离。同一抗血清（SB）可与不同的放射性配体一起用于进行N端和中央特异性放射免疫分析（RIA），这具有实际意义。中央特异性RIA在大约等摩尔基础上检测到SRIF-14和SRIF-28，而N端特异性RIA对SRIF-14具有选择性。
