title: [Ultrastructure of the L forms of Streptococcus group B].
abstract: The submicroscopic organization of the L-forms of beta-hemolytic streptococci of group B has been studied in the course of their cultivation. The L-forms of group B streptococci differ from those of group A streptococci by a higher growth rate. On the submicroscopic level, the activity of ATP-ase has been revealed on the internal side of the cytoplasmic membrane. Regularities in the localization of intramembranous particles sized 6-18 nm in the hydrophobic area of the membrane have been established by means of freezing-etching. With the adequate methods of fixation, the continuous three-layer structure of the cytoplasmic membrane can be determined in all elements of the L-form population.
mesh_terms: D000251:Adenosine Triphosphatases / Q000378:metabolism; D002462:Cell Membrane / Q000201:enzymology / Q000648:ultrastructure; D005613:Freeze Etching; D007740:L Forms / Q000201:enzymology / Q000648:ultrastructure*; D008854:Microscopy, Electron; D010088:Oxidoreductases / Q000378:metabolism; D013292:Streptococcus agalactiae / Q000201:enzymology / Q000648:ultrastructure*; D013297:Streptococcus pyogenes / Q000648:ultrastructure
chemical_list: D010088:Oxidoreductases; D000251:Adenosine Triphosphatases
vernacular_title: Ul'trastrukrua L-form streptokokka gruppy B.