Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Query: EC:3.2.1.36 (
hyaluronidase
)
4,606
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
The study of the effect of synthetic polyelectrolites of the cationic type on benzylpenicillin resistant staphylococci showed that the cation polyelectrolites induced changes in the cell membrane permeability and increased penicillin absorption by the cells thus increasing sensitivity of the penicillin-resistant staphylococci to the antibiotic. Low inhibitory effect of the polyelectrolites with respect to penicillinase and
hyaluronidase
was shown. Changes in the membrane apparatus of
staphylococcus
cells due to the effect of polyelectrolites were found.
...
PMID:[Effect of synthetic poly-electrolytes of the cationic type on staphylococcal sensitivity to benzylpenicillin]. 88 84
In 22 biological tests a study was made of the properties of 1117 strains of staphylococci isolated from patients and medical personnel surgical departments. The significance of each of the tests for species identification of staphylococci was assessed on the basis of correlation of its results with the results of study of 3 main signs characteristic of S. aureus: the presence of coagulase, anaerobic mannite fermentation, and of DNA-ase. Besides the ones pointed out the following could be considered as properties characteristic of S. aureus: flocculus-forming factor, fibrinolysin,
hyaluronidase
, lysozyme, golden pigment, tellurite-reductase, aerobic fermentation of mannite and tregalose. A standard system of species identification of staphylococci was elaborated; on its basis assessment was made of the diagnostic value of a number of simple systems used in practice for determination of
staphylococcus
species.
...
PMID:[Indentification of staphylococci of hospital origin. I. Specific identification of staphylococci]. 96 Dec 42
Staphylococcal hyaluronate lyase (
hyaluronidase
) derived from a pathogenic strain of
staphylococcus
was purified by means of salt fractionation with ammonium sulfate and gel filtration through Sephadex G-100. Most of the enzyme activity from concentrated culture supernatant fluids of staphylococci was obtained in a fraction precipitated by 90 to 100% saturation with ammonium sulfate. A small amount of enzyme was also precipitated by 80 to 90% saturation with the salt. The
hyaluronidase
-rich fractions did not contain other staphylococcal enzymes, such as coagulase, protease, lipase, and staphylokinase. These enzymes were present in the original concentrates. Molecular sieving chromatography of the partially purified enzyme by filtration through Sephadex G-100 resulted in a further increase in specific enzyme activity. However, more than one active peak was obtained after gel filtration, thus suggesting that there may be more than one molecular form of the enzyme. Immunodiffusion in agar gel of the chromatographically purified enzyme fraction, with immune serum from rabbits injected with concentrated staphylococcal culture supernatant fluids, indicated that there was one major antigen. A similar antigen, giving reactions of identity with the purified material, was present in the original culture supernatant fluid.
...
PMID:Staphylococcal hyaluronate lyase: purification and characterization studies. 430 Oct 47
The proposed method for measuring
hyaluronidase
activity of microorganism is based on prevention of hyaluronic acid clot formation with rivanol under the effect of
hyaluronidase
. This made possible the quantitative and qualitative detection of
hyaluronidase
activities of different
staphylococcus
species and strains. The maximum level of the enzyme and highest rate of its detection were typical of St. aureus. Its strains producing
hyaluronidase
in quantities of at least 0.5 IU are significantly (p < 0.01) more often isolated from medical staff.
...
PMID:[Method of quantitative determination of staphylococcal hyaluronidase activity]. 957 32