Abstract
The enzymatic and molecular properties of 14 oxacillin-hydrolyzing β-lactamases, all of them R-factor-specified, were studied, and two distinct groups were found. Four of the enzymes had a molecular weight of 24,000, were active against methicillin, and had an electrophoretic mobility of −0.1 cm/h. Eight enzymes had a molecular weight of 45,000, low activity against methicillin, and an electrophoretic mobility of +0.5 cm/h. The remaining two enzymes were similar to those of the second group in being relatively inactive against methicillin, but their molecular weight was lower (42,000) and their electrophoretic mobility was different (−0.1 cm/h). All the enzymes of both groups were sensitive to inhibition by sodium chloride. The two groups were not completely homogeneous in their enzymatic properties; seven possible subtypes could be recognized.
Full text
PDF![351](https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0010/245614/a626ac623fc0/jbacter00338-0025.png)
![352](https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0010/245614/b0cc9c2af44d/jbacter00338-0026.png)
![353](https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0010/245614/e20cc0562bca/jbacter00338-0027.png)
![354](https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0010/245614/78ff66828d5c/jbacter00338-0028.png)
![355](https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0010/245614/7d03c362d5c9/jbacter00338-0029.png)
![356](https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0010/245614/231bd47baa1a/jbacter00338-0030.png)
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- ANDERSON E. S., DATTA N. RESISTANCE TO PENICILLINS AND ITS TRANSFER IN ENTEROBACTERIACEAE. Lancet. 1965 Feb 20;1(7382):407–409. doi: 10.1016/s0140-6736(65)90004-8. [DOI] [PubMed] [Google Scholar]
- Andrews P. Estimation of the molecular weights of proteins by Sephadex gel-filtration. Biochem J. 1964 May;91(2):222–233. doi: 10.1042/bj0910222. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Dale J. W. Characterization of the -lactamase specified by the resistance factor R-1818 in E. coli K12 and other Gram-negative bacteria. Biochem J. 1971 Jul;123(4):501–505. doi: 10.1042/bj1230501. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Dale J. W., Smith J. T. A direct comparison of two unusual R-factor-mediated -lactamases. Biochem J. 1972 Jun;128(1):173–174. doi: 10.1042/bj1280173. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Dale J. W., Smith J. T. Some relationships between R-factor and chromosomal -lactamase in Gram-negative bacteria. Biochem J. 1971 Jul;123(4):507–512. doi: 10.1042/bj1230507. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Dale J. W., Smith J. T. The purification and properties of the -lactamase specified by the resistance factor R-1818 in Escherichia coli and Proteus mirabilis. Biochem J. 1971 Jul;123(4):493–500. doi: 10.1042/bj1230493. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Evans J., Galindo E., Olarte J., Falkow S. Beta-lactamase of R factors. J Bacteriol. 1968 Oct;96(4):1441–1442. doi: 10.1128/jb.96.4.1441-1442.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Haeckel R., Hess B., Lauterborn W., Wüster K. H. Purification and allosteric properties of yeast pyruvate kinase. Hoppe Seylers Z Physiol Chem. 1968 May;349(5):699–714. doi: 10.1515/bchm2.1968.349.1.699. [DOI] [PubMed] [Google Scholar]
- Hedges R. W., Datta N., Coetzee J. N., Dennison S. R factors from Proteus morganii. J Gen Microbiol. 1973 Aug;77(2):249–259. doi: 10.1099/00221287-77-2-249. [DOI] [PubMed] [Google Scholar]
- Hedges R. W., Datta N., Kontomichalou P., Smith J. T. Molecular specificities of R factor-determined beta-lactamases: correlation with plasmid compatibility. J Bacteriol. 1974 Jan;117(1):56–62. doi: 10.1128/jb.117.1.56-62.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Jenkins P. H., Drabble W. T. -lactamases of R factors derived from Shigella and Salmonella strains. J Bacteriol. 1971 Oct;108(1):159–165. doi: 10.1128/jb.108.1.159-165.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
- KNOX R., SMITH J. T. Use of cellulose acetate membranes for detecting penicillinase-producing organisms. Nature. 1961 Aug 26;191:926–927. doi: 10.1038/191926a0. [DOI] [PubMed] [Google Scholar]
- Lampen J. O. Cell-bound penicillinase of Bacillus licheniformis; properties and purification. J Gen Microbiol. 1967 Aug;48(2):249–259. doi: 10.1099/00221287-48-2-249. [DOI] [PubMed] [Google Scholar]
- Retsema J. A., Ray V. A. Correlation between the binding of beta-lactam antibiotics to Staphylococcus aureus and their physical-chemical properties. Antimicrob Agents Chemother. 1972 Sep;2(3):173–180. doi: 10.1128/aac.2.3.173. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Richmond M. H., Sykes R. B. The beta-lactamases of gram-negative bacteria and their possible physiological role. Adv Microb Physiol. 1973;9:31–88. doi: 10.1016/s0065-2911(08)60376-8. [DOI] [PubMed] [Google Scholar]
- SMITHIES O. Zone electrophoresis in starch gels: group variations in the serum proteins of normal human adults. Biochem J. 1955 Dec;61(4):629–641. doi: 10.1042/bj0610629. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Smith J. T. R-factor gene expression gram-negative bacteria. J Gen Microbiol. 1969 Jan;55(1):109–120. doi: 10.1099/00221287-55-1-109. [DOI] [PubMed] [Google Scholar]
- Staal G. E., Visser J., Veeger C. Purification and properties of glutathione reductase of human erythrocytes. Biochim Biophys Acta. 1969 Jul 8;185(1):39–48. doi: 10.1016/0005-2744(69)90280-0. [DOI] [PubMed] [Google Scholar]
- Swart A. C., Hemker H. C. Separation of blood coagulation factors II, VII, IX and X by gel filtration in the presence of dextran blue. Biochim Biophys Acta. 1970 Dec 29;222(3):692–695. doi: 10.1016/0304-4165(70)90203-5. [DOI] [PubMed] [Google Scholar]
- Witchitz J. L., Chabbert Y. A. High level transferable resistance to gentamicin. J Antibiot (Tokyo) 1971 Feb;24(2):137–139. doi: 10.7164/antibiotics.24.137. [DOI] [PubMed] [Google Scholar]
- Yamagishi S., O'Hara K., Sawai T., Mitsuhashi S. The purification and properties of penicillin beta-lactamases mediated by transmissible R factors in Escherichia coli. J Biochem. 1969 Jul;66(1):11–20. doi: 10.1093/oxfordjournals.jbchem.a129111. [DOI] [PubMed] [Google Scholar]