PubMed · 9128277
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D Lozano, M Cantero. 1997. Difference between analytical sensitivity and detection limit.. https://doi.org/10.1093/ajcp%2F107.5.619a
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Human serum albumin (HSA) preparations and HSA-containing recombinant human erythropoietin (rhEPO) formulations were analyzed by capillary zone electrophoresis. HSA was separated into several components by the addition of 1,4-diaminobutane to 20 mM sodium phosphate, pH 6.0 as electrophoretic buffer. Resolution was improved by increasing the buffer pH to 8.5. A comparative analysis of HSA preparations from three manufacturers provided evidence that this method can be used to differentiate individual preparations. The analysis of rhEPO formulations, composed largely of HSA, showed levels of heterogeneity comparable to that of HSA preparations. Electrospray ionisation mass spectrometry was used as an independent method to confirm the heterogeneous nature of HSA.
A systematic detection method for the single performance of cellulose acetate (CA) membrane isoelectric focusing to detect six different types of information on protein abnormalities was developed. High-voltage isoelectric focusing was carried out on six layers of CA membrane using a thermoelectric cooling apparatus. After electrophoresis, the proteins on the top, the third, the fourth, the fifth, and the bottom CA membrane were transferred to a polyvinylidene difluoride (PVDF) membrane by a simple contact printing procedure to detect IgM, kappa-chain, lambda-chain, IgA, and IgG, respectively. Each PVDF membrane revealed the microheterogeneity of these immunoglobulins using specified anti-serum and enzyme immunostaining. The second CA membrane was stained with Coomassie brilliant blue G250 to detect serum protein patterns. All stained membranes showed clear electrophoretic patterns of immunoglobulin microheterogeneity. By our method, immunoglobulin abnormalities in serum could be screened out using six different types of information obtained simultaneously.
An abnormal hemoglobin fraction was detected on high performance liquid chromatography profile performed for the measurement of glycated hemoglobin in a 55-year-old caucasian patient. The structural and functional studies were performed by standard techniques. Separation of hemoglobins by alkaline electrophoresis and by IEF revealed a slightly more rapid fraction than does Hb S. By acid electrophoresis, no abnormal Hb fraction could be observed. Separation of globin chains by electrophoresis demonstrated an alpha-chain variant and by chromatography, a fraction which eluted between beta and gamma globin chains. Tryptic digests and amino acid analysis have demonstrated a previously described substitution of Leu-->Arg alpha 86(F7).