Identification of proteins in human follicular fluid by proteomic profiling

被引:0
作者
Sim, Young-Jin [1 ,2 ]
Lee, Mi-Young [1 ]
机构
[1] Soonchunhyang Univ, Dept Med Biotechnol, Asan 336600, Chungnam, South Korea
[2] Mirae & Woman OBGYs Hosp, Gunsan 573370, Jeollabuk Do, South Korea
关键词
human follicular fluid; proteomics; two-dimensional gel electrophoresis; MALDI-MS;
D O I
暂无
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Human follicular fluid (HFF) is the in vivo microenvironment for oocyte maturation and includes a variety of proteins that could be involved in oocyte development and fertilization. We therefore used a proteomic approach to identify new Hi proteins. Hi from mature human follicles was obtained from five women following oocyte collection for in vitro fertilization (IVF) Ethanol-precipitated (HFF) run on two-dimensional gel electrophoresis (21 produced approximately 250 Coomassie brilliant blue-stained spots, 64 of which were identified using matrix-assisted laser clesorption/ionization-mass spectrometry (MALDI- MS). In this study, several proteins including complement factor H, inter-alpha (globulin) inhibitor H4 inter-alpha-trypsin inhibitor heavy chain H4 precursor, human zinc-alpha-2-glycoprotein chain 13, PRO2619, PRO02044, and complex-forming glycoprotein HC were new proteins that have not been previously reported in HFF using proteomic methods. Additionally, we identified alloalbumin venezia for the first time from trichloroacetic acid (TCA)-precipitated HFF These HIFF proteins could serve as new biomarkers for important human reproductive processes.
引用
收藏
页码:253 / 259
页数:7
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