Literature DB >> 14292989

PREPARATION AND PROPERTIES OF A VI ANTIGEN-DEGRADING ENZYME.

E E BAKER, R E WHITESIDE.   

Abstract

Baker, Edgar E. (Boston University School of Medicine, Boston, Mass.), and Roberta E. Whiteside. Preparation and properties of a Vi antigen-degrading enzyme. J. Bacteriol. 89:1217-1224. 1965.-Vi antigen can be hydrolyzed by an inducible enzyme produced by a microorganism isolated from soil. The organism can be identified as Bacillus sphaericus. The enzyme in the culture supernatant fluid can be concentrated and partially purified by precipitation with ammonium sulfate at 50% of saturation. The partially purified enzyme is relatively stable. Incubation of the enzyme with Vi antigen causes a rapid loss of serological activity, a decrease in viscosity, the loss of ability to precipitate albumin at pH 4.0, and the production of reducing sugar and hexosamine. Optimal conditions for enzyme action on Vi antigen are pH 8.4 and 40 C. The reaction rate is independent of the substrate concentration. Intact protein and calcium activates the Vi antigen-enzyme system. The enzyme is not inhibited by its reaction products.

Entities:  

Keywords:  BACILLUS; ENZYME INHIBITORS; ENZYMES; EXPERIMENTAL LAB STUDY; HEMAGGLUTINATION INHIBITION TESTS; HEXOSAMINES; HYDROGEN-ION CONCENTRATION; POLYSACCHARIDES, BACTERIAL; PRECIPITATION; PRECIPITIN TESTS; SALMONELLA TYPHOSA; SERUM ALBUMIN; SOIL MICROBIOLOGY; TEMPERATURE; VISCOSITY

Mesh:

Substances:

Year:  1965        PMID: 14292989      PMCID: PMC277631          DOI: 10.1128/jb.89.5.1217-1224.1965

Source DB:  PubMed          Journal:  J Bacteriol        ISSN: 0021-9193            Impact factor:   3.490


  17 in total

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Authors:  R E WHITESIDE; E E BAKER
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Authors:  F G JARVIS; M T MESENKO; J E KYLE
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4.  Specific degradation of Cryptococcus neoformans 3723 capsular polysaccharide by a microbial enzyme. I. Isolation, partial purification, and properties of the enzyme.

Authors:  H H GADEBUSCH; J D JOHNSON
Journal:  Can J Microbiol       Date:  1961-02       Impact factor: 2.419

5.  The VI antigens of the Enterobacteriaceae. I. Purification and chemical properties.

Authors:  E E BAKER; R E WHITESIDE; R BASCH; M A DEROW
Journal:  J Immunol       Date:  1959-12       Impact factor: 5.422

6.  Enzymes of Clostridium tertium: effects on blood group and virus receptor substances.

Authors:  C HOWE; J D MACLENNAN; I MANDL; E A KABAT
Journal:  J Bacteriol       Date:  1957-09       Impact factor: 3.490

7.  A Microorganism Decomposing Group-Specific A Substances.

Authors:  M W Chase
Journal:  J Bacteriol       Date:  1938-10       Impact factor: 3.490

8.  The lysis of group A hemolytic streptococci by extracellular enzymes of Streptomyces albus. II. Nature of the cellular substrate attacked by the lytic enzymes.

Authors:  M MCCARTY
Journal:  J Exp Med       Date:  1952-12       Impact factor: 14.307

9.  Studies on the chemical structure of the streptococcal cell wall. I. The identification of a mucopeptide in the cell walls of groups A and A-variant streptococci.

Authors:  R M KRAUSE; M MCCARTY
Journal:  J Exp Med       Date:  1961-07-01       Impact factor: 14.307

10.  Further studies on the chemical basis for serological specificity of Group A streptococcal carbohydrate.

Authors:  M McCARTY
Journal:  J Exp Med       Date:  1958-09-01       Impact factor: 14.307

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  3 in total

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Authors:  P A Sanford; K A Burton; P R Watson; M C Cadmus; A Jeanes
Journal:  Appl Microbiol       Date:  1975-06

2.  Isolation and purification of Flavobacterium alpha-1,3-glucanase-hydrolyzing, insoluble, sticky glucan of Streptococcus mutans.

Authors:  S Ebisu; K Kato; S Kotani; A Misaki
Journal:  J Bacteriol       Date:  1975-12       Impact factor: 3.490

3.  Interaction of Vi antigen with proteins.

Authors:  R E Whiteside; E E Baker
Journal:  J Bacteriol       Date:  1966-12       Impact factor: 3.490

  3 in total

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