Two-Dimensional Electrophoretic Studies of the Proteins and Polypeptides in Mature Pollen Grains and the Male Germ Unit of Plumbago zeylanica

Abstract

Three fractions (male germ unit [MGU]-rich, cytoplasmic-particulate and water-soluble proteins) were isolated from pollen of Plumbage zeylanica L. Proteins wer extracted using a phenol procedure and polypeptide patterns were compared on one- and two-dimensional polyacrylamide gels. The MGU-rich fraction contains the sperm and vegetative nucleus of the pollen grain and yielded 427 spots > 33 kilodaltons. The cytoplasmic-particulate fraction contained 515 spots > 33 kilodaltons. The third fraction consisted of water-soluble protein and polypeptides from the pollen cytoplasm, in which 285 spots (> 33 kilodaltons) were identified. Of 133 polypeptide spots suitable for comparison, 18 were unique to the MGU-rich fraction, 3 to the cytoplasmic-particulate fraction, 14 to the water-soluble fraction, 65 were common to two different fractions (and absent in one), and 33 were common to all three of the fractions examined.