Selected Bioinformatic Tools and MS (MALDI-TOF, PMF) Techniques Used in the Strategy for the Identification of Oat Proteins After 2-DE.

Computer analysis of protein maps obtained from the separation of proteins with two-dimensional polyacrylamide gel electrophoresis (2-DE), in combination with mass spectrometry (MS) analysis and selected bioinformatic tools is used in the strategy for the identification of oat proteins. In proteomic research the most often used MS technique is the combination of ion sources: matrix-assisted laser desorption/ionization (MALDI) and the analyzer of the time of flight (TOF), i.e.

2-DE Separation and Identification of Oat (Avena sativa L.) Proteins and Their Prolamin Fractions.

At present two-dimensional polyacrylamide gel electrophoresis (2-DE) is the most widely used proteomic tool, which enables simultaneous separation of even thousands of proteins with a high degree of resolution. The quality of 2-DE separation depends on the type of biological material used as a protein source. The presence of interfering compounds (e.

Isolation of Oat (Avena sativa L.) Total Proteins and Their Prolamin Fractions for 2D Electrophoresis.

Appropriate sample preparation is essential to obtaining good results of two-dimensional gel electrophoresis (2-DE). For various reasons (particularly phenolic compounds, proteolytic enzymes, and cell-wall mucilages) the extraction of proteins from plant material, among them oat proteins, is difficult. During isolation all soluble substances that may interfere with the analysis (especially isoelectric focusing) are removed, and proteins of interest are separated from the remains.

Proteomic analysis of albumin and globulin fractions of pea (Pisum sativum L.) seeds.

Background: Proteomic analysis is emerging as a highly useful tool in food research, including studies of food allergies. Two-dimensional gel electrophoresis involving isoelectric focusing and sodium dodecyl sulfate polyacrylamide gel electrophoresis is the most effective method of separating hundreds or even thousands of proteins. In this study, albumin and globulin tractions of pea seeds cv.