2002•中国化学快报:英文版Requires access

Spectrophotometric Study on the Interaction between Arsenazo M and Proteins

QiuLuanHU, FengLinZHAO

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Abstract

Arsenazo M could bind with bovine serum albumin to form a complex in Clark-Lube buffer at pH 2.3 and room temperature, which gives a maximum absorption peak at 625 nm with a red shift of 75 nm compared with that of Arsenazo M itself. The apparent molar absorptivity of the BSA-Arsenazo M complex is 3.21′105 L×mol-1×cm-1. The linear ranges for protein determination are wide (at least 0-100 mg/mL).

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What this paper is about

Arsenazo M could bind with bovine serum albumin to form a complex in Clark-Lube buffer at pH 2.3 and room temperature, which gives a maximum absorption peak at 625 nm with a red shift of 75 nm compared with that of Arsenazo M itself. The apparent molar absorptivity of the BSA-Arsenazo M complex is 3.21′105 L×mol-1×cm-1. The linear ranges for protein determination are wide (at least 0-100 mg/mL).

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Available abstract

Arsenazo M could bind with bovine serum albumin to form a complex in Clark-Lube buffer at pH 2.3 and room temperature, which gives a maximum absorption peak at 625 nm with a red shift of 75 nm compared with that of Arsenazo M itself. The apparent molar absorptivity of the BSA-Arsenazo M complex is 3.21′105 L×mol-1×cm-1. The linear ranges for protein determination are wide (at least 0-100 mg/mL).

Key concepts: Molar absorptivity, Chemistry, Bovine serum albumin, Absorption (acoustics), Spectrophotometry, Analytical Chemistry (journal), Chromatography, Buffer solution

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