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

Norman R. Geltz | Zendy; Scott D. Russell | Zendy

Open Access

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

Author(s) -

Norman R. Geltz,

Scott D. Russell

Publication year - 1988

Publication title -

plant physiology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 3.554

H-Index - 312

eISSN - 1532-2548

pISSN - 0032-0889

DOI - 10.1104/pp.88.3.764

Subject(s) - pollen , fraction (chemistry) , cytoplasm , spots , electrophoresis , botany , chemistry , biology , germ , sperm , polyacrylamide gel electrophoresis , biochemistry , chromatography , microbiology and biotechnology , enzyme

Three fractions (male germ unit [MGU]-rich, cytoplasmic-particulate and water-soluble proteins) were isolated from pollen of Plumbago zeylanica L. Proteins were 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 cyto-plasmic-particulate fraction contained 515 spots >33 kilodaltons. The third fraction consisted of water-soluble proteins 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.

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