[53a] β-Lactamase (Bacillus cereus)

No abstract is available for this paper.

• Publication year

  1975

• Venue

  Methods in Enzymology

• Publication date

  Unknown publication date

• Fields of study

  Biology, Chemistry

• Identifiers
  DOI 10.1016/0076-6879(75)43129-9
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar

• No claims are published for this paper.

• No concepts are published for this paper.

• Conformational changes in the extracellular beta-lactamase I from Bacillus cereus 569/H/9.

  1974cited by this paper
• Metal cofactor requirement of β-lactamase II

  1974cited by this paper
• Separation, purification and properties of β-lactamase I and β-lactamase II from Bacillus cereus 569/H/9

  1974cited by this paper
• Involvement of a carboxyl group in the active site of Bacillus cereus 569-H penicillinse ( -lactamase I).

  1973cited by this paper
• Effect of oxidation on the transition of penicillinase conformation.

  1971cited by this paper
• Amino acid composition and peptide maps of Bacillus cereus 569-H penicillinase.

  1971cited by this paper
• Chemical nature of the inactivation of Bacillus cereus penicillinase by iodine.

  1971cited by this paper
• Circular-dichroism studies on two -lactamases from Bacillus cereus.

  1971cited by this paper
• Protein and carbohydrate moieties of a preparation of -lactamase II.

  1971cited by this paper
• Interconversion of alpha- and gamma-penicillinase from Bacillus cereus 569.

  1970cited by this paper
• Sedimentation-equilibrium studies on the heterogeneity of two β-lactamases

  1970cited by this paper
• Properties of penicillinase from Bacillus cereus 569.

  1970cited by this paper
• Iodine sensitivity of Bacillus cereus penicillinase.

  1970cited by this paper
• The composition of β-lactamase I and β-lactamase II from Bacillus cereus 569/H

  1970cited by this paper
• Purification and properties of two extracellular beta-lactamases from Bacillus cereus 569-H.

  1970cited by this paper
• Chemical Structure of Bacterial Penicillinases

  1969cited by this paper
• Some properties of two cell-bound beta-lactamases from Bacillus cereus 569-H.

  1969cited by this paper
• Heritable mass conversion of a mutant penicillinase-negative culture of Bacillus cereus to a positive fully de-repressed state.

  1969cited by this paper
• THE RANGE AND SIGNIFICANCE OF VARIATIONS AMONGST BACTERIAL PENICILLINASES

  1968cited by this paper
• Purification and properties of the ?-type ?-lactamase of Bacillus cereus

  1967cited by this paper
• Some properties of two extracellular beta-lactamases from Bacillus cereus 569/H.

  1967cited by this paper
• A Suggested Phenotypic Classification and Terminology for Enzyme Mutants in Micro-Organisms

  1965cited by this paper
• Modified Substrate Specificity of Cell-bound Penicillinase

  1963cited by this paper
• Behaviour of some derivatives of 7-aminocephalosporanic acid and 6-aminopenicillanic acidas substrates, inhibitors and inducers of penicillinases.

  1962cited by this paper
• Two antigenically different states of active penicillinase.

  1958cited by this paper
• Sedimentation and diffusion of samples of penicillinase.

  1956cited by this paper
• Purification of penicillin-induced penicillinase of Bacillus cereus NRRL 569: a comparison of its properties with those of a similarly purified penicillinase produced spontaneously by a constitutive mutant strain.

  1956cited by this paper
• Crystalline bacterial penicillinase.

  1956cited by this paper
• The cell-bound penicillinase of Bacillus cereus.

  1956cited by this paper

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  2019cites this paper
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  2014cites this paper
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  1999cites this paper
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  1994cites this paper
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  1990cites this paper
• Prospective addition of β-lactamase to blood culture medium

  1988cites this paper
• Lincomycin Stimulates Synthesis ofTEM-2 3-Lactamase by Escherichia coli

  1986cites this paper
• Physicochemical properties of a β-lactamase from streptomyces UCSM-104

  1985cites this paper
• The amino acid sequence of the zinc‐requiring β‐lactamase II from the bacterium Bacillus cereus 569

  1985cites this paper
• Use of Microbial β-Lactamase to Destroy Penicillin Added to Milk

  1985cites this paper
• Purification and properties of the exocellular β-lactamase of a Actinomadura strain R39

  1982cites this paper
• Specific chemical modification of the readily nitrated tyrosine of the RTEM β-lactamase and of bacillus cereus β-lactamase I

  1982cites this paper
• Preliminary crystallographic data for β-lactamase I from Bacillus cereus 569☆

  1978cites this paper
• Chapter 25. Bacterial Resistance to β-Lactams: The β-Lactamases

  1978cites this paper
• N-(2-Furyl) acryloyl penicillin: a novel compound for the spectrophotometric assay of beta-lactamase I.

  1977cites this paper