Pig sperm tail tubulin. Its extraction and characterization.
Axonemal tubulin extracted from pig sperm tails has been characterized by one- and two-dimensional electrophoresis and by one-dimensional peptide mapping. The electrophoretic mobilities of its subunits after reduction and carboxymethylation were similar to those of the major subunits of pig brain tubulin. Sperm tail tubulin subunits also had roughly the same isoelectric points as pig brain tubulin subunits, except that they appeared to have a relatively larger tailing effect. The proteolytic cleavage pattern of the pig sperm tail beta-tubulin closely resembled those of both the tunicate (Ciona intestinalis) sperm beta-tubulin and pig brain beta-tubulin. The peptide pattern of pig sperm tail alpha-tubulin, however, was more similar to that of tunicate sperm tail alpha-tubulin than to that of pig brain alpha-tubulin. This supports the hypothesis put forward in a previous investigation [1] that functionally similar tubulins from taxonomically distant species can be more related than functionally dissimilar tubulins from the same species.
D000818:Animals; D001923:Brain Chemistry; D010450:Endopeptidases / Q000378:metabolism; D008297:Male; D008854:Microscopy, Electron; D010446:Peptide Fragments / Q000032:analysis; D012697:Serine Endopeptidases; D013082:Sperm Tail / Q000032:analysis* / Q000648:ultrastructure; D013094:Spermatozoa / Q000032:analysis*; D013552:Swine; D014404:Tubulin / Q000302:isolation & purification*
D010446:Peptide Fragments; D014404:Tubulin; D010450:Endopeptidases; D012697:Serine Endopeptidases; C028344:glutamyl endopeptidase