Isolation and partial characterization of a tubulin-like protein from human and swine synaptosomal membranes.
Synaptic membranes from human and swine brains were solubilized with 8 M urea and the proteins were reduced and alkylated. A protein was isolated from both sources and had identical amino acid compositions and molecular weights as determined by electrophoresis on polyacrylamide-sodium dodecylsulfate gels and by ion-exchange chromatography and gel filtration on Bioglas 1000. The apparent molecular weight of the protein was 53 000 on the acrylamide-sodium dodecylsulfate gels. Neither neutral sugars nor sialic acid was a significant component of the protein. When the proteins were digested with trypsin and the resultant peptides subjected to chromatography (n-butanol/acetic acid/water) and electrophoresis (pH 3.7) the peptide maps were identical. The protein comprises 1-2 percent of the total synaptosomal protein. With regard to amino acid composition, molecular weight, peptide map characteristics, behavior on DEAE-cellulose columns, electrophoretic mobility and sugar content, the synaptic protein is quite similar to the monomer of swine tubulin.
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001923:Brain Chemistry; D002241:Carbohydrates / Q000032:analysis; D002845:Chromatography; D002848:Chromatography, DEAE-Cellulose; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D008566:Membranes / Q000032:analysis; D008970:Molecular Weight; D009419:Nerve Tissue Proteins / Q000032:analysis*; D010446:Peptide Fragments / Q000032:analysis; D012794:Sialic Acids / Q000032:analysis; D013045:Species Specificity; D013552:Swine; D013574:Synaptosomes / Q000032:analysis*; D014357:Trypsin; D014404:Tubulin / Q000032:analysis* / Q000302:isolation & purification; D014508:Urea
D000596:Amino Acids; D002241:Carbohydrates; D009419:Nerve Tissue Proteins; D010446:Peptide Fragments; D012794:Sialic Acids; D014404:Tubulin; D014508:Urea; D014357:Trypsin