Disease relevance of SAB1192

• Synthesis of catalase in Staphylococcus aureus MF-31 [1].
• Simultaneous testing for clumping factor, coagulase, deoxyribonuclease, and thermonuclease was performed on 189 clinical isolates of gram-positive cocci with strong catalase activity to determine the suitability of the thermonuclease test as a routine procedure for the identification of Staphylococcus aureus [2].
• Four strains of a hitherto-unknown catalase-positive, facultatively anaerobic Corynebacterium species were isolated from the milk of sheep affected by subclinical mastitis [3].
• Double immunodiffusion tests were performed with crude extracts from various Micrococcus species and antisera against catalase of Micrococcus luteus CCM 169 [4].
• Addition of catalase to the disinfection of Escherichia coli by hydrogen peroxide, resulted in changes to the shape of the log survivor/time plots [5].

High impact information on SAB1192

• Addition of superoxide dismutase or catalase to the O2.- generating system resulted in protection of thermally stressed and nonstressed cells, with the protective effect being greater for thermally stressed cells [6].
• It was positive for urease, oxidase, catalase, glycosidases, porphyrin, and indole, and it fermented glucose and sucrose [7].
• The effects of the addition of catalase (EC 1.11.1.6) or pyruvate on the enumeration of Staphylococcus aureus in Trypticase soy broth with 10% NaCl were examined using a most-probable-number technique [8].
• Of 289 isolates of catalase-positive, gram-positive cocci, 122 were identified as S. aureus based on positive reactions in at least three of the following tests: tube coagulase, slide coagulase, DNase production, or anaerobic fermentation of mannitol [9].
• Immunochemical titration experiments with rabbit antiserum against the purified peroxisomal catalase from alkane-grown C. tropicalis indicated that the remarkable variation in the enzyme activity level on different carbon sources was ascribable to a corresponding change in the amount of the enzyme protein [10].

Chemical compound and disease context of SAB1192

• The effect of catalase on the toxicity of cadmium in cadmium-sensitive and cadmium-resistant Staphylococcus aureus [11].

Biological context of SAB1192

• To gain information on metabolic control and peroxisome biogenesis in Candida tropicalis growing on n-alkanes, cell-free translation of catalase (H2O2:H2O2 oxidoreductase, EC 1.11.1.6), a general marker enzyme of peroxisomes, was performed [10].
• When the original Delta 1058::Tn551 mutation was transduced into the hemolytic, catalase-positive variant of S6C, none of the transductants exhibited an exoprotein-deficient phenotype [12].
• The biochemical parameters such as hydroxyproline, protein, DNA, uronic acid, hexosamine, SOD, and catalase content in the granulation tissue of the healing wound revealed increased proliferation of cells involved in tissue reconstruction in PIC-treated groups when compared with OW- and CF-treated groups [13].

Anatomical context of SAB1192

• When cell-free translation was carried out with the mRNA-dependent reticulocyte lysate system, total RNA prepared from alkane-grown cells was shown to direct the synthesis of catalase subunit in vitro [10].

Associations of SAB1192 with chemical compounds

• Addition of catalase or pyruvate to the broth increased enumeration of all heat-stressed S. aureus strains tested [8].
• S. aureus strains with reduced catalase activity show greater sensitivity to oleuropein [14].
• Hydrogen peroxide resistance could be partly explained by the high catalase activity in the dead-cell fraction [15].
• These tests were as follows; catalase, oxidase, fermentation and oxidation of glucose and mannitol, v.p. and coagulase activity, heat resistance endonuclease, and lipase production [16].
• The following procedures are recommended for routine use: Idnetification of Staphylococcus sp. (clinical laboratories): microscopic observation, catalase activity, coagulase production, lysostaphin sensitivity, and (optional) facultative growth in thioglycolate medium [17].

Analytical, diagnostic and therapeutic context of SAB1192

• The assay was a modification of a 'sandwich' ELISA for the protein A of Staph. aureus, employing catalase-labelled anti-protein A antibody [18].

References