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偶氮胂III与细胞成分的结合。

The binding of arsenazo III to cell components.

作者信息

Beeler T J, Schibeci A, Martonosi A

出版信息

Biochim Biophys Acta. 1980 May 7;629(2):317-27. doi: 10.1016/0304-4165(80)90104-x.

Abstract

The Ca2+ indicator, arsenazo III, binds to subcellular fractions of rabbit skeletal muscle with sufficient affinity that in living muscle containing 1--2 mM arsenazo III, the estimated free arsenazo III concentration is only 50--200 microM; 80--90% of the bound arsenazo III is associated with soluble proteins. The binding of arsenazo III to soluble proteins decreases the optical response of the dye to Ca2+; this is due to a decrease in the affinity of the protein-bound dye for Ca2+. Approximately half of the bound arsenazo III is released from the particulate fraction and soluble proteins upon addition of 5 mM Ca2+, suggesting that the Ca-arsenazo complex has lower affinity for the protein binding sites than the free dye. The Ca2+ binding to the soluble protein fraction of rabbit skeletal muscle is attributable largely to its parvalbumin content.

摘要

钙离子指示剂偶氮胂III与兔骨骼肌的亚细胞组分结合,其亲和力足以使在含有1-2 mM偶氮胂III的活肌肉中,估计的游离偶氮胂III浓度仅为50-200 microM;80-90%的结合偶氮胂III与可溶性蛋白质相关。偶氮胂III与可溶性蛋白质的结合降低了染料对钙离子的光学响应;这是由于蛋白质结合染料对钙离子的亲和力降低所致。加入5 mM钙离子后,约一半结合的偶氮胂III从颗粒组分和可溶性蛋白质中释放出来,这表明钙-偶氮胂复合物对蛋白质结合位点的亲和力低于游离染料。兔骨骼肌可溶性蛋白质组分与钙离子的结合主要归因于其小清蛋白含量。

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