Analysis of whole-cell proteins of Streptococcus thermophilus by 2 electrophoretic methods
- Resource Type
- Authors
- C. Guimont; D. Clary; P. Bracquart
- Source
- Le Lait. 74:13-21
- Subject
- Gel electrophoresis
0303 health sciences
Streptococcus thermophilus
Strain (chemistry)
030306 microbiology
Isoelectric focusing
Biology
biology.organism_classification
03 medical and health sciences
Electrophoresis
Isoelectric point
Peptide mass fingerprinting
Biochemistry
Polyacrylamide gel electrophoresis
030304 developmental biology
Food Science
- Language
- ISSN
- 0023-7302
The protein fingerprinting obtained by 2 electrophoretic procedures was used to compare strains of Streptococcus thermophilus. Whole-cell soluble proteins were extracted and separated by 10-28% polyacrylamide gradient gel electrophoresis and pH 2.9-9.2 isoelectric focusing. Electrophoretic migration of proteins from 8 S thermophilus strains produced highly resolutive and reproducible patterns with 30-40 distinct bands on SOS-PAGE and 20-25 bands on isoelectric tocusing. Proteins of S tbermophilus display similar or almost identical patterns and major strains could be clustered with a tight relation with the strain type ATCC19258. Only strain IP 6631 showed a pattern with fewer bands in SOS-PAGE and was clustered alone. Two strains (PB 18 and CNRZ 308) appeared to be distinguished by the relative importance of a typical band. Significant variations were detected by analysis of protein banding patterns for the same strains cultured in different physiological conditions.