Analysis of differentially expressed proteins from Anopheles stephensi related with Plasmodium yoelii oocyst melanization by two-dimensional electrophoresis and MALDI-TOF-mass spectrometry
Analysis of the protein in hemolymph from Anopheles stephensi during melanotic encapsulation of Plasmodium yoelii oocysts by two-dimensional electrophoresis
Protein polypeptide contents in Lathyrus sylvestris L. treated with water stress (PEG), salt stress (NaCl) and high temperature (40℃) were analyzed with two dimensional electrophoresis.
Then the hemolymph protein was analyzed by two dimensional electrophoresis. The protein spots were visualized by Coomassie brilliant blue staining. The spots were scanned and automatically analyzed by the ImageMaster VDS CL (Amersham Pharmacia) and ImageMaster 2D Elite software (Amersham Pharmacia).
The two dimensional gel electrophoresis (2-DE) experiments was repeated for 3 times, and proved to be reliable according to the correlation coefficient analysis.
ObjectiveTo separate and identify the water soluble rat lens protein and observe the alteration of in vitro acetylated calf γ crystallin using two dimensional gel electrophoresis (2DE) integrated with mass spectrometry (MS).
Objectives: To analyze human spermatozoa membrane proteins by two dimensional gel electrophoresis and to provide a basis for drawing the protein map of normal human spermatozoa membrane proteins.
Total proteins in the pollen of Humulus scandens Lour, one of the most popular aeroallergens in China, were analyzed by two-dimensional electrophoresis in the current study.
The thermostable fraction of serum samples from patients with ovarian, uterus, and breast cancers and benign ovarian tumor was analyzed using two-dimensional electrophoresis combined with MALDI-TOF(-TOF)-mass spectrometry.
Proteins of crude extract of pea leaves were analyzed by one-and two-dimensional electrophoresis followed by Western blotting with monoclonal antibodies PY20 to phosphotyrosine proteins.