Open AccessPurification and amino acid sequence of two small, acid‐soluble proteins from Clostridium bifermentans spores
Author(s) -
CabreraMartinez Rosa Martha,
Mason James M.,
Setlow Barbara,
Waites William M.,
Setlow Peter
Publication year - 1989
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1989.tb03567.x
Subject(s) - spore , clostridium perfringens , clostridium , microbiology and biotechnology , amino acid , peptide sequence , biochemistry , clostridiaceae , bacillus (shape) , chemistry , biology , bacteria , toxin , gene , genetics
Clostridium bifermentans spores contain two major small, acid‐soluble, proteins (SASP) termed SASP‐α and β. The amino acid sequences of SASP‐α and β are almost identical, and are very similar to those of α/β‐type SASP from spores of C. perfringens and various Bacillus species. However, the C. bifermentans proteins contain an extra five amino acids in the middle of their sequence. Surprisingly, no γ‐type SASP were found in C. bifermentans or C. perfringens spores, although these are the most prominent SASP in spores of Bacillus species.