Evaluation of a capillary zone electrophoresis system versus a conventional agarose gel system for routine serum protein separation and monoclonal component typing

Capillary zone electrophoresis of serum proteins is increasingly gaining impact in clinical laboratories. During 2003, we compared the fully automated capillary electrophoresis (CE) system from Beckman (Paragon CZE 2000) with the method agarose gel electrophoresis Sebia (Hydrasis-Hyris, AGE). This new study focused on the evaluation of analytical performance and a comparison including 115 fresh routine samples (group A) and a series of 97 frozen pathologic sera with suspicion of monoclonal protein (group B). Coefficients of variation (CVs %) for the five classical protein fractions have been reported to be consistenly < 9% in within-run and < 10% in between-run imprecision studies with the Paragon 2000 system. The results of the comparison study (group A) demonstrated a good correlation between the CE system and AGE, except for beta-globulin (r = 0.65). Among the 97 pathologic serum samples (group B), there were 90 in which we detected a monoclonal protein by immunofixation (IF) (immunosubtraction (IS) was not used). AGE and Paragon 2000 failed to detect 7 and 12 monoclonal proteins, respectively, leading to a concordance to 92% for AGE and 87% for Paragon 2000 for identifying electrophoretic abnormalities in this group. Beta-globulin abnormalities and M paraprotein were well detected with Paragon 2000. Only 81% (21 vs 26) of the gammopathies were immunotyped with IS by two readers blinded to the IF immunotype. The Paragon 2000 is a reliable alternative to conventional agarose gel electrophoresis combining the advantages of full automation (rapidity, ease of use and cost) with high analytical performance. Qualified interpretation of results requires an adaptation period which could further improve concordance between the methods. Recently, this CE system has been improved by the manufacturer (Beckman) concerning the migration buffer and detection of beta-globulin abnormalities.     

Automated serum protein electrophoresis by Capillarys.

Capillary zone electrophoresis (CZE) of serum proteins is increasingly gaining impact in clinical laboratories. In this report, we evaluate automated capillary zone electrophoresis by Capillarys (Sebia, France). Within-run and between-run imprecision for the five electrophoretic fractions was <2% and <6%, respectively. Data obtained with Capillarys correlated with results obtained with agarose gel electrophoresis and Paragon CZE 2000 (Beckman Coulter, USA). Analysis of serum obtained from patients with inflammation, nephrotic syndrome, bisalbuminemia, and alpha1-antitrypsin deficiency revealed that Capillarys was able to detect these abnormalities. Two hundred thirty eight samples were analyzed by agarose gel electrophoresis, Capillarys, capillary electrophoresis using Paragon CZE 2000 system, and immunofixation. Sample selection was based on the presence of a disturbed morphology (e.g., spike) of the protein profile or hypogammaglobulinemia on agarose gel electrophoresis and/or Capillarys. Immunofixation revealed the presence of a monoclonal protein, oligoclonal bands, polyclonal pattern, and a normal profile in, respectively, 89, 66, 19, and 64 samples. With Capillarys, Paragon, and agarose gel electrophoresis, a spike and/or disturbed morphology of the profile was found in 222, 182, and 180 samples, respectively. In these samples, immunofixation was negative in 73 (33%), 46 (25%), and 39 (22%) samples, respectively. These data indicate that Capillarys has a lower specificity than agarose gel electrophoresis and Paragon 2000. Of the 89 samples with a monoclonal protein, Capillarys, Paragon, and agarose gel electrophoresis failed to detect, respectively, three, three, and one monoclonal protein(s). Interferences by radio-opaque agents, complement degradation products, fibrinogen, and triglycerides are described. In conclusion, automated capillary zone electrophoresis with Capillarys provides for reproducible, rapid, and reliable serum electrophoresis.     

Routine differential diagnosis of proteinurias by capillary electrophoresis.

Capillary electrophoresis is a relatively new analytical technique that begins to have an impact on both routine and research in clinical laboratories. Recently, a fully automated system has become commercially available (Paragon CZE 2000, Beckman, USA) for the analysis of human serum proteins. Urine protein analysis, on the other hand, is currently accomplished by electrophoresis of concentrated urine specimens. The method is used to distinguish the glomerular from the tubular proteinuria and for the identification of Bence-Jones proteins. The procedure is labor-intensive and technically demanding. We developed a technique for the serum capillary electrophoresis instrument that can also be applied routinely to the differential diagnosis of proteinurias. Overriding the programmed dilution step of the instrument, we were able to distinguish different types of proteinurias without concentration of specimens with a total protein content of 150-200 mg/l as determined by sulfosalicylic acid. The different electrophoretic patterns obtained by the capillary electrophoresis system for various specimens correlated well with established techniques (Hydragel Proteinurie Kit, Sebia, France). The method is applicable for routine analysis of urinary proteins. It is reliable, less expensive and faster than the conventional methods (electrophoretic or immunonephelometric) used today for the differentiation of proteinurias, and it can be used as a quick screening test.     

Comparison of two methods for the quantification and identification of hemoglobin variants

BackgroundThe Sebia Capillarys 2, a capillary electrophoresis method, was compared to a high performance liquid chromatography (HPLC) and electrophoresis at alkaline and acid pH for the presumptive identification and quantitation of hemoglobin variants.MethodsThe concordance of hemoglobin variant identification on the Sebia Capillarys 2 with the combination of HPLC and electrophoresis at alkaline and acid pH was evaluated by analyzing samples on both systems. The quantification, expressed as % of total hemoglobin, of the common hemoglobin variants on the Capillarys 2 and the Bio Rad VARIANT II β thalassemia methods were compared.ResultsThe % hemoglobin variant results for the two methods were similar for HbS and slightly different for HbC and D Punjab and significantly different for HbE. The Sebia Capillarys 2 correctly identified a number of hemoglobin variants.ConclusionThe Sebia Capillarys 2 is suitable for the presumptive identification and quantification of hemoglobin variants producing results comparable with existing HPLC and electrophoresis methods.     

Separation of serum proteins by automated capillary zone electrophoresis.

Capillary zone electrophoresis (CZE) of serum proteins is increasingly gaining impact in clinical laboratories. Two automated multichannel instruments dedicated to the separation of serum proteins have become available over the last 6 years, the Paragon CZE 2000 (Beckman Coulter, CA, USA) and, more recently, the Capillarys (Sebia, France). This review focuses on the performance of these commercial instruments to separate serum proteins in a clinical laboratory setting. The utility of CZE to recognize various dysproteinemias and to detect and identify monoclonal proteins will be described and systematically reviewed. The reader will be provided with a summation and an understanding of CZE-specific interference.     

Fully automated analysis of Carbohydrate-Deficient Transferrin (CDT) by using a multicapillary electrophoresis system

BACKGROUND: The techniques universally believed as most reliable for determination of Carbohydrate-Deficient Transferrin (CDT) are HPLC and capillary electrophoresis (CE). Recently a reagent kit for CDT analysis to be used in a multicapillary electropherograph has been introduced. The present work was aimed at a validation of this new commercial system by application of the analytical chemistry parameters and by comparison with validated CE and HPLC methods. METHODS: One hundred forty serum samples were analyzed with multicapillary CE (Capillarys, Sebia, France) using kit reagents (CAPILLARYS CDT assay), with single capillary electropherograph (P/ACE MDQ, Beckman Coulter, USA) using an original method developed by our group and with HPLC, performed on a gradient HPLC (Shimadzu Europe, Germany), using column and reagents provided in kit (ClinRep, Recipe, Germany). RESULTS: The separation efficiency of the multicapillary system was about 15,000 theoretical plates/column. The resolution of the transferrin isoforms ranged from 1.23 to 1.67. The variation coefficient was < 10% in both intra-run and between run tests. The correlation of results of multicapillary CE with those obtained with single CE and HPLC was statistically significant. CONCLUSIONS: The multicapillary system shows high productivity with good analytical performances; however, a confirmation of positive results with an alternative method is required.     

Simple method for quantification of Bence Jones proteins

BACKGROUND: Quantification of free monoclonal light chains in urine [Bence Jones proteins (BJPs)] is used to diagnose multiple myeloma and to evaluate response to treatment. We have developed and evaluated an optimized approach for quantification of BJPs. METHODS: High-resolution gel electrophoresis of unconcentrated urine and albumin calibrators was carried out on Sebia's Hydrasys instrument with Hydragel HR agarose gels. After staining with acid violet, the gels were scanned densitometrically. The staining intensities of BJP bands relative to the staining intensities of albumin solutions were used to determine the BJP concentrations. Results for patient samples were compared with conventional agarose gel electrophoresis on concentrated samples. RESULTS: The relationships between staining intensity and the protein concentrations of albumin and BJPs were linear up to protein concentrations of approximately 2000 mg/L. The detection limit was approximately 20 mg/L. The interassay imprecision (CV) was approximately 8% (n = 23, duplicate analysis), and the results (y) showed a close positive relationship to the comparison method: slope = 0.82 (confidence interval, 0.75-0.88); y-intercept = 34 (-14 to 81) mg/L; n = 29; r(2) = 0.96. CONCLUSIONS: Agarose gel electrophoresis of unconcentrated urine samples together with a series of albumin calibrators followed by acid violet staining and densitometric scanning is sufficiently reproducible and sensitive to quantify clinically relevant BJPs.     

Ten electrophoretic methods compared with a selected method for quantifying lactate dehydrogenase isoenzymes in serum

Using the Selected Method of McKenzie and Henderson (Selected Methods Clin Chem 1983;10:59-67) as a reference method, we compared the performance of 10 commercially available methods for determination of lactate dehydrogenase (LD, EC 1.1.1.27) isoenzymes. Results were expressed as percentage of total LD activity, as determined with two different types of densitometers shown to have an average difference less than 1.4% for each isoenzyme. All methods gave generally comparable results, as judged by Bland-Altman plots and correlation analyses. However, in general, estimates by the commercial methods for LD-1, LD-2, and LD-3 were lower, and for LD-4 and LD-5 were higher than with the Selected Method. The overall CV was less than 20% for all methods and isoenzymes, except for LD-4 and LD-5 by the Beckman Paragon, Helena LD-VIS, Gel LDH, Gel PC, and Iso Dot, Gelman LDH Isozyme, and Sebia Hydragel assays, for which it was greater than 20%. Overall, accuracy was best with the Helena Iso Dot and LD-VIS assays, followed by the Corning LD Flur assay; accuracy was poorest with the Gelman LDH Isozyme, Sebia Hydragel, and Beckman Paragon assays.     

Analytical evaluation of a new capillary electrophoresis method for carbohydrate-deficient transferrin measurement

BACKGROUND: Carbohydrate-deficient transferrin (CDT), the sum of a- and disialotransferrin, is considered the most efficient routine biological marker of alcohol abuse. In recent years, methods based on capillary zone electrophoresis (CZE) have been developed using specialized monocapillary systems. These are characterized by a high analytical detection level, counterbalanced by a poor productivity. We evaluated a new CZE method for CDT measurement on the Sebia Capillarys, an eight-capillary system developed for routine serum capillary electrophoresis. METHODS: Precision and possible biases due to abnormal (low or high) transferrin levels or lipemic samples were assessed. Exactitude and precision were tested by comparison with a HPLC procedure acknowledged to be the most reliable to date. The validity of the manufacturer's cut-off was checked by measuring CDT in a population comprising abstaining patients, moderate alcohol consumers and alcohol abusers. Lastly, the method was compared to the routine %CDT TIA and N Latex CDT methods. RESULTS: The imprecision was 18.5% at the minimum detection level and decreased to 6.1% for high CDT values. No significant shift in the CDT results was observed in relation to abnormally low or high serum transferrin, or in lipemic samples. A high level of concordance was observed with the HPLC method used as reference. The results were strongly correlated with both other routine methods (r>0.90). The diagnostic values were comparable to the literature data, even if differences in the studied populations make difficult a direct comparison of the results. Our data suggested that the cut-off could be raised from 1.3% to 1.4% to reduce the number of false positive values without loss of diagnostic efficiency. CONCLUSIONS: This Capillarys method from Sebia showed good precision as compared to those published using other CZE methods. Capillarys method correlated well with HPLC and two routine methods. However, we noticed significant bias at low CDT concentrations. Therefore, with the advantage of high throughput and full automation, these results indicate that the new method is a consistent alternative to the other methods proposed for routine CDT measurement.     

Evaluation of a new Sebia isoelectrofocusing kit for alpha 1-antitrypsin phenotyping with the Hydrasys System.

BACKGROUND: Laboratory evaluation of alpha 1-antitrypsin (A1AT) deficiency is generally performed by determination of A1AT concentrations and identification of specific allelic variants by phenotyping. For this purpose, we evaluated a new Hydragel 18 A1AT Isofocusing kit on the semi-automatic Hydrasys System (Sebia) for the determination of A1AT phenotypes by isoelectrofocusing on ready-to-use agarose gels with specific immunological detection. METHODS: Serum samples from 66 patients were analysed with this new kit in comparison with the conventional and manually performed isoelectrofocusing method on polyacrylamide gels with Coomassie Blue staining. RESULTS: A1AT phenotypes showed comparable iso-electrofocusing patterns in both systems. The good within-gel reproducibility of this kit was demonstrated using two normal serum samples (M1 and M1M2 phenotypes) and six pathological serum samples with different phenotypes (MS, SS, SZ, MZ, ZZ). A sensitivity study was undertaken by performing serial dilutions on a serum with a ZZ phenotype containing 0.27 g/L A1AT. The detection limit was 0.050 g/L. CONCLUSIONS: This new method is highly specific, rapid and simple to perform. It improves identification of not only the most common but also various rare A1AT phenotypes. It appears to be suitable for routine analysis and screening applications in a clinical laboratory setting.     

Computer-supported detection of M-components and evaluation of immunoglobulins after capillary electrophoresis

BACKGROUND: Electrophoresis of serum samples allows detection of monoclonal gammopathies indicative of multiple myeloma, Waldenstr?m macroglobulinemia, monoclonal gammopathy of undetermined significance, and amyloidosis. Present methods of high-resolution agarose gel electrophoresis (HRAGE) and immunofixation electrophoresis (IFE) are manual and labor-intensive. Capillary zone electrophoresis (CZE) allows rapid automated protein separation and produces digital absorbance data, appropriate as input for a computerized decision support system. METHODS: Using the Beckman Paragon CZE 2000 instrument, we analyzed 711 routine clinical samples, including 95 monoclonal components (MCs) and 9 cases of Bence Jones myeloma, in both the CZE and HRAGE systems. Mathematical algorithms developed for the detection of monoclonal immunoglobulins (MCs) in the gamma- and ss-regions of the electropherogram were tested on the entire material. Additional algorithms evaluating oligoclonality and polyclonal concentrations of immunoglobulins were also tested. RESULTS: CZE electropherograms corresponded well with HRAGE. Only one IgG MC of 1 g/L, visible on HRAGE, was not visible after CZE. Algorithms detected 94 of 95 MCs (98.9%) and 100% of those visible after CZE. Of 607 samples lacking an MC on HRAGE, only 3 were identified by the algorithms (specificity, 99%). Algorithms evaluating total gammaglobulinemia and oligoclonality also identified several cases of Bence Jones myeloma. CONCLUSIONS: The use of capillary electrophoresis provides a modern, rapid, and cost-effective method of analyzing serum proteins. The additional option of computerized decision support, which provides rapid and standardized interpretations, should increase the clinical availability and usefulness of protein analyses in the future.     

Capillary zone electrophoresis of serum proteins: effects of changed analytical conditions.

Analytical conditions in a system for capillary zone electrophoresis (Beckman Paragon CZE 2000) were originally selected to allow serum protein separation into five discrete protein zones, corresponding to those of conventional clinical electrophoresis. To improve the system's performance, new analytical conditions have been made available. We compared the two sets of conditions ("new" = y; "old" = x) for possible variations of results caused by the change. One hundred thirteen serum samples, covering wide intervals of values, were assayed on two twin instruments working under the old and the new conditions; results were assessed statistically and graphically. Possible clinical significance of differences was checked by comparison with the biological variation-based quality specifications for bias. Statistically significant (y-x) differences were observed for the alpha1-, alpha2- and beta-globulin zones; clinically significant differences were observed for all the zones, with the exception of the gamma-globulin zone. Therefore, old/new regression equations were calculated, whose reliability was assured by the wide interval of values, by the large sample size, and by the low dispersion of single values around the mean concordance estimates. Such equations may be used to convert "old" into "new" reference values, and for the intercomparison of patient results obtained under different analytical conditions.     

Automated multicapillary electrophoresis for analysis of human serum proteins

BACKGROUND: We evaluated a new, automated multicapillary zone electrophoresis (CE) instrument (Capillarys), 4.51 software version; Sebia) for human serum protein analysis. METHODS: With the Capillarys beta1-beta2+ reagent set, proteins were separated at 7 kV for 4 min in 15.5 cm x 25 micro m fused-silica capillaries (n = 8) at 35.5 degrees C in a pH 10 buffer with online detection at 200 nm. Serum samples with different electrophoretic patterns (n = 265) or potential interference (n = 69) were analyzed and compared with agarose gel electrophoresis (AGE; Hydrasys)-Hyrys, Hydragel protein(e) 15/30 reagent set; Sebia). RESULTS: CVs were <3.5% for albumin, <11% for alpha(1)-globulin, <4.1% for alpha(2)-globulin, <7.4% for beta-globulin, and <5.8% for gamma-globulin (3 control levels); measured throughput was 60 samples/h. In patients without paraprotein (n = 116), the median differences between CE and AGE were -5.4 g/L for albumin, 4.0 g/L for alpha(1)-globulin, 0.7 g/L for alpha(2)-globulin, 0.6 g/L for beta-globulin (P <0.001 for all fractions), and -0.1 g/L for gamma-globulin (not significant). More samples had at least one gamma-migrating peak detected by CE (n = 135 vs 130; paraprotein detection limit, approximately 0.5-0.7 g/L), but fewer were quantified (n = 84 vs 91) because of gamma- to beta-migration shifts. There was a 1.2 g/L median difference between CE and AGE for gamma-migrating paraprotein quantification (n = 69; P <0.001). Several ultraviolet-absorbing substances (lipid emulsion, hemoglobin) or molecules (contrast agent, gelatin-based plasma substitute) induced CE artifacts. CONCLUSIONS:The Capillarys instrument is a reliable CE system for serum protein analysis, combining advantages of full automation (ease of use, bar-code identification, computer-assisted correction of alpha(1)-globulins) with high analytical performances and throughput.     

全自动毛细管电泳仪在珠蛋白生成障碍性贫血筛查中的应用

目的评价法国Sebia公司Capillarys 2全自动毛细管电泳仪在珠蛋白生成障碍性贫血筛查中的应用。方法采集2011年8～12月经血分析(红细胞平均体积小于80fL,红细胞平均血红蛋白浓度小于26pg的8岁以上患者)筛选后的292份标本用法国Sebia公司Capillarys 2全自动毛细管电泳仪对入选标本进行血红蛋白(Hb)毛细管电泳、血清铁、铁蛋白检查,同时作α-及β-珠蛋白生成障碍性贫血基因检查。结果 (1)共检测了292例临床标本,符合α-珠蛋白生成障碍性贫血表型者36例,β-珠蛋白生成障碍性贫血表型者135例。同时出现α-及β-珠蛋白生成障碍性贫血表型者2例。(2)高压毛细管电泳法用于α-珠蛋白生成障碍性贫血诊断的灵敏度为86.11%,特异度为98.37%,准确度为95.60%,阳性预测值为93.94%,阴性预测值为96.03%。(3)高压毛细管电泳法用于β-珠蛋白生成障碍性贫血诊断的灵敏度为97.04%,特异度为98.35%,准确度为97.66%,阳性预测值为98.50%,阴性预测值为96.75%。HbA2值大于4.0%时,β-珠蛋白生成障碍性贫血基因法检测阳性率达100.00%。结论法国Sebia公司Capillarys 2全自动毛细血管电泳仪对Hb区带分辨及定量准确度高,可为Hb病(包括珠蛋白生成障碍性贫血及异常Hb病)的初筛提供快速的诊断依据。     

Analysis of inflammatory response in human plasma samples by an automated multicapillary electrophoresis system.

A new automated multicapillary zone electrophoresis instrument with a new high-resolution (HR) buffer (Capillarys with HR buffer) for analysis of human plasma proteins was evaluated. Albumin, alpha(1)-antitrypsin, alpha(1)-acid glycoprotein, haptoglobin, fibrinogen, immunoglobulin (Ig)A, IgG and IgM were determined nephelometrically in 200 patient plasma samples. The same samples were then analyzed on the Capillarys system (Sebia, Paris, France). The albumin concentration from the nephelometric determination was used for quantification of the individual peaks in the capillary electrophoresis (CE) electropherogram. There was strong linear correlation between the nephelometric and electrophoretic determination of alpha(1)-antitrypsin (R(2) = 0.906), alpha(1)-acid glycoprotein (R(2) =0.894) and haptoglobin (R(2) = 0.913). There was also good correlation between the two determinations of gamma-globulins (R(2) = 0.883), while the correlation was weaker for fibrinogen (R(2) = 0.377). The Capillarys instrument is a reliable system for plasma protein analysis, combining the advantages of full automation, good analytical performance and high throughput. The HR buffer in combination with albumin quantification allows the simultaneous quantification of inflammatory markers in plasma samples without the need for nephelometric determination of these proteins.     

尿蛋白电泳在肾脏疾病诊断中的临床应用

目的根据蛋白质分子量不同,采用十二烷基硫酸钠琼脂糖凝胶(SDS-AGE)对尿蛋白进行电泳,以判断肾脏疾病的受损部位及病变程度。方法采用法国Sebia公司HYDRASYS全自动电泳分析仪对104例肾脏疾病患者尿液进行电泳分析。结果根据尿蛋白电泳图谱扫描测定,104例尿蛋白电泳显示10例为生理性蛋白尿,37例为肾小球性蛋白尿,12例为肾小管性蛋白尿,45例为混合性蛋白尿,其中20例同时做肾活检,系膜增生性肾小球肾炎18例,膜增生性肾小球肾炎2例,SDS-AGE尿蛋白电泳结果与肾活检结果基本相符。结论琼脂糖尿蛋白电泳技术简便快速,无创伤,对早期肾损伤的诊断,肾脏损伤部位分析,指导治疗和判断预后有较高的价值。     

Precision and long-term stability of capillary electrophoresis measurement of serum protein zones

BACKGROUND: Analytical evaluations of an available system for capillary zone electrophoresis (CZE) of serum protein have been reported. However, data concerning long-term precision and stability of the system, operated under routine conditions, are lacking. We report data from an internal quality control (QC) scheme, obtained over a 1-year period. METHODS: Measurements were done with a pair of instruments (Beckman Paragon CZE 2000 system), each equipped with seven capillaries. After preliminary (1 month) assessment of possible inter-capillary and inter-instrument variations, the QC material (a home prepared serum pool stored in the frozen state) was assayed daily over a 1-year period. RESULTS: Maximum inter-capillary and inter-instrument differences were 3.1% and 2.4%. No significant trend was observed for daily values (205 measurements over 1 year); in the same period overall imprecision values (CV) were in the interval 1.2% (albumin) to 3.2-6.1% (globulin zones). Mean monthly imprecision (CV) values were in the interval 1.1% (albumin) to 5.2% (globulin zones). There was no significant trend of monthly means with time. The observed imprecision values were within the biological variation-derived goals for imprecision. CONCLUSIONS: It is concluded that the assessed analytical instruments, operated in routine conditions, show long-term stability and imprecision consistent with the clinical use of the results produced.     

免疫固定电泳在多发性骨髓瘤中的诊断价值

目的探讨免疫固定电泳（IFE）在多发性骨髓瘤（MM）诊断中的价值及临床意义。方法采用法国SebiaHydrasys全自动电泳分析仪对临床提出申请的患者的血清和尿液标本同时进行免疫固定电泳,并回顾性分析其实验室检查资料。结果 62例IFE阳性的病人经临床诊断证实,其中MM患者30人,骨髓瘤19人,MM合并其它癌症者3人,原发性巨球蛋白血症1人,骨髓纤维化1人。在所检出的M蛋白中,Kappa（κ）型20例,Lambda（λ）型38例,κ合并λ型（κ＆λ）4例。结论免疫固定电泳是诊断MM的一个灵敏度高、特异性强的较好方法,它降低了MM的误诊率和漏诊率,提高了MM诊断的准确性,并且在病情监测、疗效评估和预后判断上也发挥着不可替代的作用。     

血清蛋白电泳分布规律对多种疾病的诊断价值

目的探讨血清蛋白电泳的分布特点及对多种不同疾病的临床诊断价值,并进一步分析其在不同肾病中的临床及实验室检查的特点。方法采用法国Sebia全自动毛细管电泳仪,对多种疾病和正常对照组血清进行电泳,分析其分布规律。结果各组疾病与对照组比较,除β1球蛋白差异无统计学意义(P>0.05)外,白蛋白、α1球蛋白、α2球蛋白、β2球蛋白、γ球蛋白以及M蛋白均有显著性差异(P<0.01),"山形峰"、"β-γ"桥、宽γ、"M"带显著;在肾病分型各组中肾病综合征中α2球蛋白、β2球蛋白显著高于其他组(P<0.05)。结论血清蛋白电泳分布规律分析对于各类疾病的临床诊断具有重要的参考价值。