Search results for "Peanut agglutinin"
showing 3 items of 3 documents
Topology of the 10 subunits within the decamer of KLH, the hemocyanin of the marine gastropod Megathura crenulata.
2002
Immunoelectron microscopy has been performed using negatively stained immune complexes of keyhole limpet hemocyanin isoform 1 (KLH1) decamers and a functional unit-specific monoclonal antibody anti-KLH1-c1. The antibody links hemocyanin molecules at both the collar and the collarless edge of the decamer, indicating a peripheral localization of functional units c. In isoform 2 (KLH2) the positions of functional units c have been identified with the peanut agglutinin (PNA), which has previously been shown to exclusively bind to KLH2-c. Ferritin linked to PNA was used to visualize labeled molecules electron microscopically. The pattern of labeling also indicates a peripheral localization of th…
Comparative histological, histochemical, immunohistochemical and biochemical studies on oestrogen receptors, lectin receptors, and Barr bodies in hum…
1986
The present study performed on a total of 567 cases of human female breast cancer compares the results of the biochemical assay (dextran-coated charcoal assay = DCC) for oestrogen receptor (ER) with those of several morphological methods developed for the detection of the ER or for the prediction of prognosis by use of other systems (FSA = fluorescent ligand binding assay, ER-ICA = monoclonal antibody assay for ER, LRA = lectin receptor assay using peanut agglutinin, and Barr body estimation). Whereas no correlation at all was observed among the results of the DCC and those of the FSA and Barr body estimation, the ER-ICA and the LRA showed an unanimous tendency towards higher values of ER w…
Primary structure and unusual carbohydrate moiety of functional unit 2-c of keyhole limpet hemocyanin (KLH)
1999
Abstract The complete amino acid sequence of the Megathura crenulata hemocyanin functional unit KLH2-c was determined by direct sequencing and matrix-assisted laser desorption ionization mass spectrometry of the protein, and of peptides obtained by cleavage with EndoLysC proteinase, chymotrypsin and cyanogen bromide. This is the first complete primary structure of a functional unit c from a gastropod hemocyanin. KLH2-c consists of 420 amino acid residues. Circular dichroism spectra indicated approx. 31% β-sheet and 29% α-helix contents. A multiple sequence alignment with other molluscan hemocyanin functional units revealed average identities between 41 and 49%, but 55% in case of Octopus he…