小鼠血清淀粉样蛋白P成分（SAP）的体内合成与分解代谢研究。
Studies of the in vivo synthesis and catabolism of serum amyloid P component (SAP) in the mouse.
作者信息
Baltz M L, Dyck R F, Pepys M B
出版信息
Clin Exp Immunol. 1985 Jan;59(1):235-42.
The production of mouse serum amyloid P component (SAP), a major acute phase protein of liver origin, was studied immunocytochemically using the peroxidase staining technique. SAP was not detectable in the cytoplasm of hepatocytes from normal, unstimulated mice, nor was it observed before 24 h after an acute phase stimulus. 125I-labelled mouse SAP was cleared from the plasma in vivo with a half-life of 7.0-8.25 h in all animals studied including: normal mice of different strains with different genetically determined plasma SAP concentrations; mice undergoing acute phase responses with greatly elevated plasma SAP levels and mice with casein-induced amyloidosis. The circulating level of SAP is thus independent of its rate of clearance and catabolism and is determined by the rate of synthesis and/or secretion of SAP.
采用过氧化物酶染色技术，通过免疫细胞化学方法研究了小鼠血清淀粉样蛋白P成分（SAP）的产生，SAP是一种主要由肝脏产生的急性期蛋白。在正常、未受刺激的小鼠肝细胞胞质中未检测到SAP，在急性期刺激后24小时内也未观察到。在所有研究的动物中，包括不同品系、具有不同基因决定的血浆SAP浓度的正常小鼠；经历急性期反应、血浆SAP水平大幅升高的小鼠以及酪蛋白诱导的淀粉样变性小鼠，体内125I标记的小鼠SAP从血浆中清除，半衰期为7.0 - 8.25小时。因此，SAP的循环水平与其清除率和分解代谢率无关，而是由SAP的合成和/或分泌率决定。
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