Aminoacid composition and hydrophobicity index of mitochondrial polypeptides

Abstract
The aminoacid composition of protein stained bands in polyacrylamide gels, after electrophoresis of proteins from inner mitochondrial membranes, was investigated hydrolyzing directly the gel slices. The Hydrophobicity Index of 18 prominent polypeptide bands was calculated after their aminoacid analysis. The polypeptides less related to the membrane have low hydrophobicity as inferred from their Hydrophobicity Indexes.
Keywords:
Amino Acids/isolation and purification, Animals, Electrophoresis, Liver/analysis/metabolism, Mitochondria, Peptides/isolation and purification, Polyacrylamide Gel, Rats, Water/metabolism
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