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Specific antibodies to two plant, hormones, namely indole-3-acetic acid and gibberellic acid, were produced in rabbits which were immunized with conjugates of either hormone to hemocyanin. The specific antibodies obtained were used for assaying the hormones by several immunological assays. The most sensitive assay reported in this paper, for the determination of indole-3-acetic acid and gibberellic acid, is the inhibition of inactivation of modified bacteriophage. For this assay conjugates of either hormone with bacteriophage T4 were prepared and characterized. Such chemically modified bacteriophages were completely inactivated by the respective specific antiserum and this inactivation was inhibited by the free hormone. The specificity of the antibodies produced was tested by a series of cross-reactions. There was no immunological cross-reaction between the two hormones which can, therefore, be determined independently. However, antibodies to indole-3-acetic acid cross-reacted with chemically related compounds such as indole-acetyl-ε-amino caproic acid, tryptamine and tryptophan. The immunological specificity of different gibberellins tested was found to be in good correlation with the biological specificity. [ABSTRACT FROM AUTHOR]

1. Tryptic hydrolysates of denaturated glutamic-aspartic transaminase fractionated on a Sephadex G-25 column, gave an elution diagram containing six main fractions. When peptide maps were developed from the transaminase digest 37 spots were detected on the paper sheet. 2. It was demonstrated that the transaminase fractions (groups of peptides) as well as some of the individual peptides eluted from the map spots, possessed immunological activity. This was proved by their capacity to interact with rabbit pig heart antienzyme and rabbit antiserum against the pig-heart whole tryptic transaminase hydrolysate as well as to inhibit the homologous transaminase-antitransaminase reaction. Higher immunological reactivity was found among peptides moving faster in electrophoresis and chromatography. 3. The catalytic activity of rabbit transaminase (heart, liver, skeletal muscles), was inhibited to a substantial degree by the rabbit anti-pig heart transaminase. The above enzymes however, as was otherwise expected, gave negative precipitin reactions with antitransaminase. A comparative study of the reactivity between transaminases from pig, ox and rabbit and rabbit anti-transaminase against pig and ox heart enzymes as well as against pig-heart whole tryptic transaminase hydrolysate is presented here. [ABSTRACT FROM AUTHOR]

In a preceding publication Le Minor and Staub [8] predicted from phagic and immunological studies, that the repeating unit, of the group D2 polysaccharide should be: [This equation cannot be presented in ASCII format] In this paper the specific polysaccharide was prepared according to Freeman's technique and hydrolysed. High yields of 3 oligosaccharides have been obtained whose analysis gave: [This equation cannot be presented in ASCII format] Periodate oxydation of the polysaccharide intact or degraded by Slight hydrolysis (N CH3COOH, 4 hours at 100°), confirmed these data and showed that tyvelose is linked to carbon 3 of mannose. No O-acetyl was found. Immunological data showed that tyvelose was the immunodominant sugar for both factors (9) and 46. No other analysis of these factors was possible since we did not possess oligosaccharides containing tyvelose. The position d the different factors of Salmonella strasbourg ((3), (9), (10), 46) on the polysaccharide is schematised on Fig. 6. [ABSTRACT FROM AUTHOR]