目的探讨一种新型淀粉样变性诊断标记物131I-SAP的制备方法及其应用安全性。方法应用Iodogen法对SAP标准品进行131I标记;纸层析法测定131I-SAP的标记率与放射化学纯度。将131I-SAP分别于4℃和37℃新鲜人血清中0h，24h，48h，72h和96h，测定放射化学纯度，评价其体外稳定性。对131I-SAP进行热原、异常毒性等安全性实验。结果131I-SAP的标记率为70.6%，96h后的放射化学纯度仍大于90%。热原、异常毒性实验均为阴性。结论131I-SAP具有较好的体外稳定性，并且无热原及明显毒性反应，适合进一步临床实验及应用的安全性。
魏海亮
,
闫平
,
张建华
,
刘萌
,
康磊
,
张丽
,
郭凤琴
,
张春丽
,
王荣福
. 131I-SAP的制备及应用安全性研究[J]. 标记免疫分析与临床, 2013
, 20(3)
: 179
-181
.
DOI: 10.11748/bjmy.issn.1006-1703.2013.03.018
Objective To prepare a novel imaging agent of 131I-SAP targeting amyloidosis, and evaluate its security for further clinical application. Methods Standard sample of SAP was radiolabeled with 131I by Iodogen method. The labeling efficiency and radiochemical purity of 131I -SAP were calculated by the paper chromatography. The in vitro stability of 131I-SAP under different conditions(4 ℃ and 37℃) were determined at 0, 24, 48, 72 and 96 h respectively. Pyrogen and toxicity tests were also performed. Results The labelingefficiencies of 131I-SAP reached 70.6%, and the radiochemical purity was above 90% at 96 hours. The safety experiments showed that 131I-SAP was free of pyrogen and toxicity. Conclusion 131I-SAP is stable in vitro, and free of pyrogen and toxicity, which may be suitable for further clinical application.
[1] Pepys M B, Booth D R, Hutchinson W L, et al. Amyloid P component. A critical review[J]. Amyloid:The Journal of protein folding disorders,1997, 4(4):274-295.
[2] Tennent G A, Dziadzio M, Triantafilidou E, et al. Normal circulating serum amyloid P component concentration in systemic sclerosis[J]. Arthritis Rheum,2007,56(6):2013-2017.
[3]Hawkins P N, Myers M J, Epenetos A A, et al. Specific localization and imaging of amyloid deposits in vivo using 123I-labeled serum amyloid P component[J]. J Exp Med,1988,167(3):903-913.
[4] Hazenberg B P, van Rijswijk M H, Piers D A, et al. Diagnostic performance of 123I-labeled serum amyloid P component scintigraphy in patients with amyloidosis[J]. Am J Med,2006,119(4):355.e15-e24.
[5]Hawkins P N, Aprile C, Capri G, et al. Scintigraphic imaging and turnover studies with iodine-131 labelled serum amyloid P component in systemic amyloidosis[J]. Eur J Nucl Med, 1998,25(7):701-708.
[6]魏海亮,张春丽,王荣福,等.碘标记血清淀粉样P成分在动物模型中的体内分布及显像研究[J].中华核医学杂志,2011, 31(6):410-413.
[7] Schaadt B K, Hendel H W, Gimsing P, et al. 99 Tc m -Aprotinin scintigraphy in amyloidosis [J]. J Nucl Med, 2003, 44(2):177-183.
[8]Eguchi M, Takizawa H, et al. Detection of cardiac calcinosis in hemodialysis patients by whole body scintigraphy with 99m-Technetium methylene diphosphonate[J]. Am J Nephrol, 2000, 20(4): 278-282.
[9]Kazama J J, Arakawa M, Gejyo F. Synovial inflammatory cells captured 131I-beta 2-microglobulin in patients with dialysis related amyloidosis[J]. Amyloid, 1998, 5(1):24–29.
[10]Dezutter N A, Landman W J, Jager P L. Evaluation of 99mTc-MAMA-chrysamine G as an in vivo probe for amyloidosis[J]. Amyloid, 2001, 8(3):202-214.
[11] Botto M, Hawkins P N, Bickerstaff MC, et al. Amyloid deposition is delayed in mice with targeted deletion of the serum amyloid P component gene[J]. Nature Med, 1997, 3(8):855-859.
[12] Hachulla E,Grateau G. Diagnostic tools for amyloidosis[J]. Joint Bone Spine,2002,69(6):538-545.
[13] Bodin K,Ellmerich S,Kahan M C,et al. Antibodies to human serum amyloid P component eliminate visceral amyloid deposits[J].Nature,2010,468(7320):93-97.
