Analysis of representative strains of the eight human serotypes of by polyacrylamide gel electrophoresis identified 36 to 40 polypeptides for each strain. At least 80% of the peptides were common among strains, but unique major peptides were identifiable in ureaplasmic types. Type 1 had a polypeptide of 85,000 daltons, type 3 had a polypeptide of 72,000 daltons, type 5 had a polypeptide of 64,000 daltons, and type 8 had a polypeptide of 95,000 daltons. The unique polypeptides in types 1 and 8 were identified as membrane components. Two common major components of 44,000 and 70,000 daltons were observed. Several components were common to some, but not all, serotypes. Patterns obtained from strains were strikingly different from the patterns of and Isoelectric focusing demonstrated a unique membrane protein for type 1 at pK 6.4, whereas type 8 possessed an assembly of five unique proteins at pK 7.0. Ureaplasmata were strongly similar to each other by isoelectric focusing, but strikingly different from members of the other genera studied. Although a filtered, strongly buffered dialysate medium with 1% serum and 30 mM urea was used both to maximize yields and to minimize contamination, minor contaminants were detected, which comigrated with horse transferrin (pK 6.0) and cytochrome c (molecular weight, 14,000). The similarities of the polypeptide patterns of strains affirm their close relationships to each other, in contrast to the diversity shown in the genus and our recognition of type-specific membrane peptides will enhance the identification of serotypes and the classification of strains.


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