%0 Journal Article %A Watabe, Kazuhito %A Takesue, Mariko %A Yamashita, Tamae %A Ichikawa, Tomio %A Kondo, Masaomi %T Purification and Characterization of Cytoplasmic Proteins Synthesized in the Developing Forespores of Bacillus subtilis during Sporulation %D 1983 %J Microbiology, %V 129 %N 8 %P 2501-2507 %@ 1465-2080 %R https://doi.org/10.1099/00221287-129-8-2501 %I Microbiology Society, %X Forespores of Bacillus subtilis 60015 were isolated from sporulating cells at t 5 and were incubated with an amino acid mixture containing [14C]phenylalanine. Three species of 14C-labelled cytoplasmic proteins synthesized in the forespores were purified to homogeneity by gel filtration in the presence of detergents and by ion-exchange chromatography. The molecular weights of the purified proteins, called A, B and C, were estimated by SDS-PAGE as 24200, 11500 and 12700, respectively. Protein B contained remarkably high amounts of tyrosine (23·8%) and alanine (22·8%), and proteins A and C contained relatively high amounts of glutamate + glutamine, glycine, and alanine (10·4 to 13·3%). The synthesis of these proteins can provide markers for the control events in the forespore compartment during sporulation. %U https://www.microbiologyresearch.org/content/journal/micro/10.1099/00221287-129-8-2501