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
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.