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R Utzinger

Publications and source records attributed to R Utzinger.

8 recordsLinked to original sources
PubMed1977

Immunochemical studies on acetylornithine 5-aminotransferase from Pseudomonas aeruginosa.

Mouse antibodies with specificity towards acetylornithine 5-aminotransferase (ACOAT) from Pseudomonas aeruginosa were used to study the structural similarities of several isofunctional enzymes from different sources. With the antibody directed against ACOAT, the amounts of enzyme present in cells grown under different conditions were determined. These experiments established that the enzyme is induced by arginine and is subject to repression by carbon sources.

Arginine↗
PubMed1975

Hapten-immunological studies on mescaline.

Antibodies with mescaline binding specificity were raised in rabbits by immunization with conjugates of bovine serum albumin with mescaline or its analogue 3,4,5-trimethoxyphenylacetic acid. Immunized rats were given mescaline and their behavior was compared to that of non-immunized controls.

Absorption↗
PubMed1975

F antigen. III. Immunological and biological properties.

Relationship of the isoforms of F antigens from A2G and CBA inbred mouse strains have been worked out in detail in respect to their immunogenicity. Mice from several inbred strains have been shown to possess the ability of forming anti-F upon stimulation with xenogeneic F antigens from certain species. An immunoelectrophoretic method for sensitive quantitation of the antigen is described. During human ontogenesis the antigen appears very early. It could never be detected in serum except in cases of acute liver disease. A small fragment set free under denaturing conditions showed the ability of inhibiting precipitation of the complete antigen by antibody. The F protein seems to be a vehicle for this small fragment possessing haptenic properties and probably being responsible for the universal cross-reactivity.

Animals↗
PubMed1975

F antigen. II. Chemical and physical properties.

Physical and chemical properties of the liver-specific F antigen suggested a model for the labile quarternary structure of the protein. The native molecule showed a size slightly larger than 60,000 dalton (d), which was reduced to about 40,000 d under acidic conditions. Breaking of hydrogen bonds by chaotropic treatment resulted in the release of components of 30,000, 7,000 and 2,000 d. The smallest component was split to fragments of about 1,000 d by the reducing action of sulfhydryl compounds.

Animals↗