Preparation and Properties of a Vi Antigen-Degrading Enzyme

Baker, Edgar E.; Whiteside, Roberta E.

doi:10.1128/jb.89.5.1217-1224.1965

Cited by 13 publications

(5 citation statements)

References 9 publications

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“…It seemed possible that the material remaining at the origin represented a core structure not attacked by the enzyme, since Baker and Whiteside (1965) observed that the enzyme did not bring about complete hydrolysis. Exhaustively degraded Vi antigen was concentrated on an Amicon filter.…”

Section: Resultsmentioning

confidence: 99%

“…Enzymes. The Vi antigen-degrading enzyme was isolated from cultures of B. sphaericus ATCC 17932, by the method of Baker and Whiteside (1965). Vi enzyme assays were carried out at 40°with the substrate in a standard buffer containing 0.033 m Tris (pH 8.2) and 1 mM CaCl2.…”

Section: Methodsmentioning

confidence: 99%

“…To test this possibility, Baker et al (1959) developed an extremely mild procedure for extracting Vi antigen from cells. Baker and Whiteside (1965) also isolated a soil microorganism, Bacillus sphaericus, which makes an inducible enzyme capable of degrading the Vi antigen under mild conditions. The work to be presented in this paper was undertaken to examine the enzymatic degradation of the Vi antigen and to determine whether nonuronic acid substances were present in this material.…”

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confidence: 99%

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Pectate lyase and polygalacturonate lyase activity in a Vi antigen-degrading enzyme preparation

McNicol¹,

Baker²

1970

Biochemistry

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Section: Resultsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

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confidence: 99%

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Pectate lyase and polygalacturonate lyase activity in a Vi antigen-degrading enzyme preparation

McNicol¹,

Baker²

1970

Biochemistry

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“…Deacetylated Vi was obtained by treating Vi with 0.1 N NaOH at room temperature (15). Enzymatically degraded Vi was made by the procedure previously described (2). O antigen was prepared from water extracts of acetonekilled S. typhosa 0-901.…”

Section: Methodsmentioning

confidence: 99%

Interaction of Vi Antigen with Proteins

Whiteside

Baker

1966

J Bacteriol

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Purified Vi antigen (Vi) mixed in equal amounts with bovine serum albumin (BSA) or human y globulin (HGG) at pH values above 4.7 formed a complex which was not precipitated by trichloroacetic acid or tungstic acid. At pH values below 4.7, the interaction between Vi and either BSA or HGG produced insoluble complexes except when excess Vi antigen was present. When sufficient Vi was present at the lower pH values, the soluble complex was not precipitated by trichloroacetic acid. Other acid polysaccharides tested did not form trichloroacetic acid-soluble complexes with BSA. When subjected to immunoelectrophoresis, the Vi-BSA complex migrated in agar at a rate different from that of either BSA or Vi alone. The complex reacted with both Vi and BSA antiserum. The addition of either BSA or Vi antiserum to a Vi-BSA complex resulted in dissociation of the complex and precipitation of either Vi or BSA, depending upon the antiserum used. Vi antigen mixed with purified 0 antigen from Salmonella typhosa formed a complex which migrated in agar at a rate different from that of either component alone when subjected to immunoelectrophoresis.

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“…Hydrolyzing N-Acetylglucosaminyl Ribitol Teichoic Acid-Peptidoglycan Complex The methods essentially followed those of Baker and Whiteside [2] and Kotani et al [14], used for isolating soil bacteria degrading Vi antigen and serologically active mycobacterial and corynebacterial polysaccharides, respectively. Soil specimens were incubated at 29 C and pH 7.2 in a minimal medium containing 0.1% (NH4)2SO4, 0.2% K2HPO4, 0.0005% MgSO4.7H20 and S. aureus cell wall lysate [ref.…”

Section: Isolation From Soil Of a Microorganism Capable Ofmentioning

confidence: 99%

Microorganism Capable of Decomposing N‐Acetylglucosaminyl Ribitol Teichoic Acid of Staphylococcus aureus

Iwata

Tochikubo

Kato

et al. 1976

Japanese Journal of Microbiology

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Enzyme(s) capable of decomposing N-acetylglucosaminyl ribitol teichoic acid prepared from the cell wall of Staphylococcus aureus FDA 209 P was obtained from the culture supernatant of a gramnegative, rod-shaped, spore-forming soil bacterium.Properties of the bacterium were very similar to those of Bacillus circulans.Bacterial cell wall teichoic acids are phosphodiester-linked polymers of glycerol phosphate or ribitol phosphate. The diester linkage had been thought to be resistant to hydrolytic enzymes [13]. Recently, however, Wise et al [21] have reported two different teichoic acid hydrolases produced by a gram-negative soil bacterium and by Marburg strain of Bacillus subtilis. They found the enzymes, which were called "teichoicase", in cell-free extracts of these two organisms. Since the enzymes responsible for hydrolysis of teichoic acids are useful tools to study the structure and function of these acids, we have also searched for bacteria which produce teichoic acid hydrolyzing enzyme(s) using a different screening method. The present paper deals with the isolation of another soil bacterium which can hydrolyze teichoic acid. Partial characterization of the bacterium and the teichoic acid hydrolyzing enzyme(s) excreted into the culture medium are reported. MATERIALS AND METHODSSoluble complex of teichoic acid-peptidoglycan.The cells of Staphylococcus aureus strain FDA 209 P were grown with shaking in nutrient broth supplemented with 0.5% glucose at 37 C for 48 hr, and disrupted by a Braun mechanical cell homogenizer (model MSK). Purified cell wall was prepared by a procedure similar to that described previously [8]. The purified cell wall preparation (1.7 g) was suspended in 60 ml of 0.025 M acetate buffer, pH 4.7, containing 1 mg of Chalaropsis enzyme (endo-N, 6-O-diacetylmuramidase) [9] kindly donated by Dr. P.A. Miller (Lederle Laboratory Division, American Cyanamid Company, New York). A few drops of chloroform were added as a preservative and the suspension was incubated at 37 C. During digestion, aliquots were withdrawn, immediately inactivated by heating at 100 C for 5 min, and the reducing groups were determined. Incubation was continued until the maximum liberation of reducing groups. Usually, 48 hr were sufficient. The whole reaction mixture was then heated at 100 C for 5 min, and veronal buffer, pH 8.5, was added so that the final concentration of the buffer was 0.01 Min a total volume of 240 ml. After the addition of 130 mg of Flavobacterium L-11 enzyme [12] (furnished from Kyowa Hakko Kogyo Co., Ltd., Tokyo, lot No. 32) and a few drops of chloroform, Requests for reprints should be addressed to Dr.

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Preparation and Properties of a Vi Antigen-Degrading Enzyme

Cited by 13 publications

References 9 publications

Pectate lyase and polygalacturonate lyase activity in a Vi antigen-degrading enzyme preparation

Pectate lyase and polygalacturonate lyase activity in a Vi antigen-degrading enzyme preparation

Interaction of Vi Antigen with Proteins

Microorganism Capable of Decomposing N‐Acetylglucosaminyl Ribitol Teichoic Acid of Staphylococcus aureus

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