title: Amino-acid sequence data of beta-tubulin from Physarum polycephalum myxamoebae.
abstract: Starting with 7.7 mg of a beta-tubulin isolated from myxamoebae of the slime mould Physarum polycephalum, 90% of the sequence has been determined by the Edman degradation of peptides generated by cyanogen bromide, trypsin and Staphylococcus aureus protease. Differences to other beta-tubulins are mainly conservative and spread evenly throughout the chain except for a high concentration at the C-terminus. The Physarum beta-tubulin shows most homology to Chlamydomonas beta-tubulin (90.5%) and least homology to yeast beta-tubulin (S. cerevisiae, 73.4%). Two tryptic peptides were isolated in approximately equal quantities which were identical except in one position (S/ALTVPELTQRMFDA) showing that at least two beta-tubulins are present in myxamoebae. However, since this was the only heterogeneity found, these beta-tubulins are probably very similar.
mesh_terms: D000595:Amino Acid Sequence; D002851:Chromatography, High Pressure Liquid; D003488:Cyanogen Bromide; D010450:Endopeptidases; D005656:Fungal Proteins / Q000302:isolation & purification*; D006868:Hydrolysis; D010804:Physarum / Q000032:analysis*; D012697:Serine Endopeptidases; D014357:Trypsin; D014404:Tubulin / Q000302:isolation & purification*
chemical_list: D005656:Fungal Proteins; D014404:Tubulin; D010450:Endopeptidases; D012697:Serine Endopeptidases; C028344:glutamyl endopeptidase; D014357:Trypsin; D003488:Cyanogen Bromide