Disease relevance of pbg

• The pbg gene was subcloned into pBR322 and was successfully expressed in Escherichia coli, suggesting that the pbg gene codes for a beta-galactosidase of C. perfringens [1].
• The ganglioside was found to be resistant to neuraminidase (Clostridium perfringens), beta-hexosaminidase (jack bean), and beta-galactosidase [2].

High impact information on pbg

• All gangliosides were resistant to beta-galactosidase but sensitive to Clostridium perfringens sialidase, indicating the absence of terminal galactose residues and sialidase-resistant sialic acid moieties [3].
• Southern analysis revealed that the colA gene is located 6.5 kb downstream of the pbg gene in the chromosome of C. perfringens [4].
• The transcript contained a message for ORF54, located upstream of the pbg gene in the chromosome, indicating that ORF54 and the pbg gene comprise one operon (pbg operon) [5].
• Expression of the pbg operon was induced by lactose at the transcriptional level [5].
• It produced galactose on incubation with beta-galactosidase, and N-acetyllactosamine and aspartic acid on incubation with 4-L-aspartylglycosylamine amindo hydrolase [6].

Biological context of pbg

• The promoter structure of the pbg operon was characterized by many palindrome structures and direct repeats, which suggests that there might be some catabolite regulation of the expression of the pbg operon in C. perfringens [5].

Associations of pbg with chemical compounds

• 2. The purified acid form appeared as a single band of protein (Mr = 28,000) on electrophoresis in the presence of sodium dodecyl sulphate, suggesting that forms A3 and A2 are multimeric forms of beta-galactosidase A1 [7].
• 4. The data suggest that the sialic acids present in the multimeric forms are involved in the aggregation of the acidic form of beta-galactosidase [7].

References