Development of an improved fractionation of the human plasma proteome by a combination of abundant proteins depletion and multi-lectin affinity chromatography

被引:8
|
作者
Gbormittah, Francisca O. [1 ,2 ]
Hincapie, Marina [3 ]
Hancock, William S. [1 ,2 ]
机构
[1] Northeastern Univ, Barnett Inst, Boston, MA 02115 USA
[2] Northeastern Univ, Dept Chem & Chem Biol, Boston, MA 02115 USA
[3] Genzyme Corp, Framingham, MA 01701 USA
关键词
HUMAN-SERUM; M-LAC; MASS-SPECTROMETRY; CANCER; IMMUNODEPLETION; GLYCOSYLATION; GLYCANS; ALBUMIN; GLYCOPROTEINS; PSA;
D O I
10.4155/bio.14.217
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Aim: Current analytical tools lack the required capacity to reduce the complexity of the plasma proteome and identify low-level proteins of clinical interest. Hence, the need to develop a fractionation approach to provide adequate throughput for a clinical study and minimize the loss and improve the detection of low abundance proteins. Materials & methods: We present the development of an analytical platform that combines the depletion of 12 high abundance proteins and multi-lectin affinity chromatography (12P-M-LAC) fractionation. Results & conclusion: We validated the highly specific, stable and robust 12P-M-LAC platform using human plasma. An improved enrichment of low abundance proteins and glycoproteins with minimum sample loss was achieved demonstrating the suitability of this platform in future biomarker discovery studies.
引用
收藏
页码:2537 / 2548
页数:12
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