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Comparative Study
. 1989 Oct 1;52(1-2):139-43.
doi: 10.1016/0378-1097(89)90185-7.

Purification and amino acid sequence of two small, acid-soluble proteins from Clostridium bifermentans spores

R M Cabrera-Martinez  1 , J M Mason, B Setlow, W M Waites, P Setlow
Affiliations
Comparative Study

Purification and amino acid sequence of two small, acid-soluble proteins from Clostridium bifermentans spores

R M Cabrera-Martinez et al. FEMS Microbiol Lett. .

Abstract

Clostridium bifermentans spores contain two major small, acid-soluble, proteins (SASP) termed SASP-alpha and beta. The amino acid sequences of SASP-alpha and beta are almost identical, and are very similar to those of alpha/beta-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 gamma-type SASP were found in C. bifermentans or C. perfringens spores, although these are the most prominent SASP in spores of Bacillus species.

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