Variability of a water-insoluble protein fraction from maize pollen

An aqueous-insoluble protein fraction has been extracted from maize pollen using a solvent containing phenol, acetic acid, and water (2:1:1, w/v/v) in 3 M urea. The solvent extracted 26% of the total protein from the pollen. The proteins of this fraction were subjected to polyacrylamide gel electrophoresis using the same solvent system. A comparison of the banding patterns of 10 inbred lines and a commercial hybrid revealed a high level of variability among the lines. Some variability was also observed within lines. The degree of variability was similar to that observed in maize seed proteins extracted with the same solvent. However, a comparison of overall banding patterns and individual band intensity differences among the lines examined revealed no apparent homology between the proteins of the two tissues.