Molecular diversity of rat brain proteins as revealed by proteomic analysis.

Multiple protein expression forms (MPEFs) presenting splicing forms or co- and posttranslation modifications, account for the vast diversity, the myriad of gene products and clearly indicate problems which proteomics research is facing. In the present study, we generated a rat brain map representing MPEFs by the use of an analytical method based on two-dimensional electrophoresis combined with mass spectrometry. Forty-nine individual proteins were selected that showed more than two spots, resulting altogether into a total number of 357 expression forms.

Proteomic determination of metabolic enzymes of the amnion cell: basis for a possible diagnostic tool?

Amniocentesis is a valuable and standard procedure for prenatal diagnosis of genetic or inborn errors of metabolism. Amnion cells are cultivated and chromosomes or proteins can be examined to provide molecular diagnosis. Mainly individual proteins are searched for based upon pedigrees and/or anamnesis.

Evidence for existence of thirty hypothetical proteins in rat brain.

BACKGROUND: The rapid completion of genome sequences has created an infrastructure of biological information and provided essential information to link genes to gene products, proteins, the building blocks for cellular functions. In addition, genome/cDNA sequences make it possible to predict proteins for which there is no experimental evidence. Clues for function of hypothetical proteins are provided by sequence similarity with proteins of known function in model organisms.

Enrichment of low-abundance brain proteins by preparative electrophoresis.

Detection of low-copy-number gene products is essential for the development of novel drugs, however, it represents a major drawback of proteomics and simultaneously a scientific challenge. We studied the enrichment of rat brain cytosolic proteins by preparative electrophoresis using the PrepCell apparatus. The electrophoresis was performed in the presence of 0.

Proteomic analysis of the fetal brain.

We applied proteomic technologies to analyze the human fetal brain. Such an analysis could provide us with important information on the development of the early neuronal life in healthy and diseased states. The proteins from the cerebellum of control subjects were analyzed by two-dimensional electrophoresis and identified by matrix-assisted laser desorption/ionization-mass spectrometry on the basis of peptide mass fingerprinting, following in-gel digestion with trypsin.