Enzymatic Activity of Coagulase-positive &lt;i&gt;Staphylococcus aureus &lt;/i&gt;Strains Isolated from Patients and Healthy Carriers

Kedzia, W; Musielak, Małgorzata; Kędzia, Bogdan; Koniar, H; Pniewska, E.

doi:10.1159/000161915

Pathobiology

1966

DOI: 10.1159/000161915

|View full text |Cite

Enzymatic Activity of Coagulase-positive <i>Staphylococcus aureus </i>Strains Isolated from Patients and Healthy Carriers

W Kedzia¹,

Małgorzata Musielak²,

Bogdan Kędzia³

et al.

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...

Citation Types

Supporting

Mentioning

Contrasting

Year Published

1968

1969

Publication Types

Select...

Article3

Relationship

Self Cite0

Independent3

Authors

Journals

Cited by 3 publications

(3 citation statements)

References 8 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Phosphatase has sometimes been implicated as a virulence factor for Staphylococcus aureus (9,10,13). The organism produces both an acid and alkaline phosphatase, the latter being repressed by inorganic phosphate in the growth medium (19).…”

mentioning

confidence: 99%

Staphylococcal Acid Phosphatase: Extensive Purification and Characterization of the Loosely Bound Enzyme

Malveaux

Clemente

1969

J Bacteriol

View full text Add to dashboard Cite

Acid phosphatase of Staphylococcus aureus PS55 was eluted from the surface of these cells with 1.0 M KCl at pH 8.5 by gentle agitation at 25 C and was purified 44fold (51% recovery) by two cycles of dialysis and gel filtration. The eluted enzyme which had a 280/260 (nm) absorbancy ratio of 0.71 required at least 0.5 M salt solution for solubilization; however, most of the purified product which had a 280/260 (nm) absorbancy ratio of 1.72 was soluble in dilute buffer solution [0.01 M tris(hydroxymethyl)aminomethane chloride, pH 8.5]. Purified acid phosphatase appeared homogeneous according to the criteria of gel filtration, starch-block electrophoresis, and analytical ultracentrifugation. In a starch block, migration was toward the cathode at pH 8.0. Maximal activity occurred at pH 5.2 to 5.3 and salt concentration had little effect on phosphatase activity up to 1.0 M KCl or NaCl. Progressive loss of enzymatic acitivity occurred at higher salt concentrations. Molecular weight of purified acid phosphatase was estimated to be 58,000.

show abstract

mentioning

confidence: 99%

Staphylococcal Acid Phosphatase: Extensive Purification and Characterization of the Loosely Bound Enzyme

Malveaux

Clemente

1969

J Bacteriol

View full text Add to dashboard Cite

show abstract

“…Observed variations in "isoenzyme" patterns and LDH activity among pathogens and nonpathogens may also provide some insight into the inherent virulence of these organisms. Tvler (7) showed that coagulase-positive strains of staph-ylococci have greater LDH activity than nonpathogenic strains, and Kedzia et al (9) noted greater succinic dehydrogenase activity among the pathogenic strains, e.g., those most often associated with severe sepsis. It was our intention to correlate LDH activity and electrophoresis patterns with phage grouping.…”

mentioning

confidence: 99%

Lactate Dehydrogenase Activity in Certain Strains of Staphylococcus aureus

Stockland

Clemente

1968

J Bacteriol

View full text Add to dashboard Cite

Lactate dehydrogenase (LDH) was studied in phage-propagating strains 29, 3A, 6, 81, and 42D of Staphylococcus aureus selected from the five groups in the International-Blair series. Cells were cultivated in Brain Heart Infusion (Difco) under nearly anaerobic conditions and were harvested near the end of the log phase. LDH activity-was maximal at the end of the exponential growth period and was measured spectrophotometrically by reduction of p-nitro-blue tetrazolium, with phenazine methosulfate as a coupling agent. Crude enzyme extracts were prepared both by an acetone extraction technique and by sonic treatment. LDH activity for these enzyme preparations was determined by the colorimetric method mentioned and also by measuring the rate of nicotinamide adenine dinucleotide reduction at 340 m,. The order of activity observed, by use of both assay methods, was 29 > 81 > 6 > 3A > 42D. LDH forms (possibly isoenzymes) for each of 15 strains, which represent the five phage-propagating groups of the International-Blair series, were separated by acrylamide gel electrophoresis. Five forms were distinguished and arbitrarily numbered on the basis of their rate of migration, no. 5 being the slowest component. No one strain had more than four, nor fewer than two, LDH forms. Form 3 appeared in 13 of the 15 strains and was followed in frequency by no. 2, 1, 4, and 5.

show abstract

“…Resistance of staphylococci to H202, especially at lower treatment temperatures, might be re-lated to catalase activity, since variability in catalase activity between strains has been demonstrated (8,9). It has also been shown that staphylococci with higher catalase activities were able to grow in the presence of higher concentrations of H202 at 37 C than were cultures with lower activities (9, 10).…”

mentioning

confidence: 99%

Influence of Catalase Activity on Resistance of Coagulase-positive Staphylococci to Hydrogen Peroxide1

Amin

Olson

1968

Applied Microbiology

View full text Add to dashboard Cite

Catalase activities of intact cells and cell-free extracts of coagulase-positive staphylococcal cultures 105B and 558D isolated from milk, culture 25042 from a clinical source, and Staphylococcus aureus 196E were determined at 32.2 C. Cultures were treated with 0.025 and 0.05 % hydrogen peroxide at 37.8 and 54.4 C and without hydrogen peroxide at 54.4 C to determine the relationship between catalase activity and resistance to these treatments. The relationship held true for cultures 105B and 196E; culture 105B had the lowest catalase activity and lowest resistance to H202 at 37.8 C, whereas S. aureus 196E possessed a high catalase activity and was most resistant at 37.8 C. Catalase activities of cell-free extracts of cultures 25042, 558, and 196E were similar, but resistance to H202 at 37.8 C was greater for culture 196E. The lower resistance of culture 25042 was related to low catalase activities of whole cells of this culture, which were only one-third that of wholecells ofculture 196E. Culture 558 was least resistant to heattreatmentat 54.4 C and showedthegreatest sensitivityto added H202 at this temperature.

show abstract

scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.

Contact Info

hi@scite.ai

10624 S. Eastern Ave., Ste. A-614

Henderson, NV 89052, USA

Blog Terms and Conditions API Terms Privacy Policy Contact Cookie Preferences Do Not Sell or Share My Personal Information

Made with 💙 for researchers

Part of the Research Solutions Family.

Enzymatic Activity of Coagulase-positive <i>Staphylococcus aureus </i>Strains Isolated from Patients and Healthy Carriers

Cited by 3 publications

References 8 publications

Staphylococcal Acid Phosphatase: Extensive Purification and Characterization of the Loosely Bound Enzyme

Staphylococcal Acid Phosphatase: Extensive Purification and Characterization of the Loosely Bound Enzyme

Lactate Dehydrogenase Activity in Certain Strains of Staphylococcus aureus

Influence of Catalase Activity on Resistance of Coagulase-positive Staphylococci to Hydrogen Peroxide1

Contact Info

Product

Resources

About