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Based on the enhancement of resonance light scattering (RLS) of m-nitrophenylfluorone -Mo(VI) complex by protein, a novel method for protein microdetermination in Tween 20 microemulsion has been developed. Under optimum condition, the linear ranges of bovine serum albumin are 0 ~ 0.03 μg?mL-1 with detection limits of 3.10 ng?mL-1. Most of amino acids and metal ions do not interfere. The method can be applied to determination of residual protein in penicillin Na salt and penicillin G potassium salt samples with satisfactory results.
Based on the enhancement of resonance light scattering (RLS) of m-nitrophenylfluorone-Mo (VI) complex by protein, a novel method for protein microdetermination in Tween 20 microemulsion has been developed. Under optimum conditions, the linear ranges of bovine serum albumin are 0 to 0.03 μg · mL-1 with detection limits of 3.10 ng · mL-1. Most of amino acids and metal ions do not interfere. The method can be applied to determine the residual protein in penicillin Na salt and penicillin G potassium salt samples with satisfactory results.