UTILIZATION OF PATTERNS OF BIOTINYL-POLYPEPTIDES AS A PROMISING ANALYTICAL TARGET FOR BACTERIAL IDENTIFICATION

Citation
Lc. Au et al., UTILIZATION OF PATTERNS OF BIOTINYL-POLYPEPTIDES AS A PROMISING ANALYTICAL TARGET FOR BACTERIAL IDENTIFICATION, Analytical biochemistry, 226(2), 1995, pp. 232-234
Citations number
13
Categorie Soggetti
Biology
Journal title
ISSN journal
00032697
Volume
226
Issue
2
Year of publication
1995
Pages
232 - 234
Database
ISI
SICI code
0003-2697(1995)226:2<232:UOPOBA>2.0.ZU;2-Y
Abstract
The family of biotin enzymes, which are involved in carboxylation, tra nscarboxylation, and decarboxylation reactions in cells, is essential and conserved for bacteria. The prosthetic group biotin is stably link ed to the biotinyl-polypeptide by an amide bond. Since avidin interact s with biotin in an irreversible manner, the patterns of biotinyl-poly peptides for bacterial cells could be revealed by probing them with an avidin-enzyme complex in Western blots of total cellular proteins. In this way, the family of commonly existing gene products of bacteria c ould be monitored and compared without the use of specific DNA probes, oligonucleotide primers, or antibodies. In this study, this approach was tested and it was found that different species of bacteria showed different patterns of biotinyl-polypeptides. Our results indicate that patterns of biotinyl-polypeptides can be a promising analytical targe t for bacterial identification. (C) 1995 Academic Press, Inc.