New procedures for preparation and isolation of conjugates of proteins and a synthetic copolymer of D-amino acids and immunochemical characterization of such conjugates.

Highly specific ligand-receptor interactions generally characterize surface recognition reactions. Such processes can be simulated by streptavidin-biotin-specific binding. Biotin lipids have thus been synthesized, and their interaction with streptavidin (or avidin) at the air-water interface was directly shown by measurement of surface pressure isotherms and fluorescence microscopy. These proteins interact with the biotin lipid monolayer via specific binding or nonspecific adsorption. Both phenomena were clearly distinguished by use of the inactivated form of streptavidin. The binding of fluorescein-labeled streptavidin to monolayers was also directly observed by fluorescence microscopy. The fluorescence of the protein domains is directly related to the state of polarization of the exciting light. This anisotropy can only be explained by the formation of oriented two-dimensional biotin lipid-streptavidin domains.

Interaction between biotin lipids and streptavidin in monolayers: formation of oriented two-dimensional protein domains induced by surface recognition.

A mouse monoclonal antibody (MoAb), reactive with a repetitive carbohydrate epitope on lentil-lectin adherent glycoproteins present on the surface and in the secretions of Taenia saginata cysticerci, was used in the construction of a diagnostic ELISA assay to detect these glycoproteins in the serum of T. saginata infected cattle. The MoAb was used as the trapping layer and subsequently bound glycoprotein was revealed using the same MoAb and biotinylated peroxidase-streptavidin complex as the developing system. The assay was suitably specific. Exceptionally low background values were obtained with sera from animals with a range of commonly occurring tropical parasitic infections, including Taenia hydatigena, Echinococcus granulosus and Fasciola gigantica. The minimal detection level was approximately 200 live cysticerci in cattle. Parasite derived glycoprotein could be detected in serum from about 4-5 weeks post-infection onwards and was associated with a current infection, as drug treatment of infected cattle to kill the cysticerci resulted in the disappearance of these components from the circulation, while the titre of anti-parasite antibody remained high. The same assay also detected Taenia solium cysticercosis in humans.

Specific detection of circulating surface/secreted glycoproteins of viable cysticerci in Taenia saginata cysticercosis

https://febs.onlinelibrary.wiley.com/doi/pdf/10.1016/0014-5793%2876%2980445-0

Affinity cytochemistry: the localization of lectin and antibody receptors on erythrocytes via the avidin-biotin complex.

A novel procedure for labeling immunoglobulins by conjugation to oligosaccharide moieties.

Publisher Summary The purification of avidin by affinity chromatography is based upon the unusually strong complex formed by this protein with polymer-bound biotin. The first specific purification of avidin was performed by McCormick, who passed an avidin solution of 10% purity over columns containing biotin esterified to cellulose. However, both yield and resolution were poor. Porath improved the technique by attaching biotin to Sephadex by means of a phenyl glyceryl spacer. Excellent purification was achieved, but the yield was low and the column could not be regenerated. The best method to date was accomplished by coupling biocytin to Sepharose. A 4000-fold purification was obtained in a single step, and 90% of the avidin activity was recovered directly from egg white. Two disadvantages are evident with this system. First, biocytin is not available commercially. Second, denaturing conditions were necessary in order to elute the protein from the column, although the entire activity could be restored upon regeneration.

[20] Insolubilized biotin for the purification of avidin

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[20] Insolubilized biotin for the purification of avidin