Slope analysis of the postoperative CEA time course and its possible application as an aid in diagnosis of disease progression in gastrointestinal cancer.
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Biomedical subjects
Publications and source records attributed to F A Anderer.
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A crude membrane fraction isolated from mouse tumour cells was treated with various chemicals. The effects on the immunogenicity of the membrane sample were tested in syngeneic mice for tumour protection, using a challenge dose of 10(5) viable tumour cells. Best protection was obtained after immunization of mice with a membrane sample modified with dimethylsulphate. Up to 60% of the animals remained tumour free, and the tumour-bearing animals showed a greatly increased mean survival time. The post-challenge sera contained no detectable amounts of cytotoxic antibodies. The membrane sample isolated from tumour cells which had been modified with dimethylsulphate showed less immunogenicity than the modified cells or the membrane fraction from unmodified cells.
Serial determinations of CEA concentrations in serum were performed postoperatively in 303 patients with histologically confirmed adenocarcinoma of the gastrointestinal tract. The trend of the time course of computerised CEA curves made early diagnosis of recurrence or metastases possible. Diagnosis of recurrence by means of a rise in CEA concentration preceded positive clinical diagnosis by up to 10 months. In all 26 cases confirmation was obtained by second-look operation or other diagnostic means. Analysis of serial CEA measurements made it possible to distinguish between generalised metastasization and local recurrence of the tumour, on the one hand, and limited metastasization at the site of recurrence, on the other.
Mouse tumour cells were treated with various chemical modifiers. The number of modifying groups per cell was determined with labelled reagents. The effects of the different modifying groups on the immunogenicity of the tumour cells was tested in syngeneic mice for tumour protection using a challenge dose of viable cells at 1000 or 10,000 time LD100. Best protection was obtained after immunization of animals with tumour cells modified with dimethylsulphate or acetic anhydride, or with glutardialdehyde-fixed cells treated with a carbodiimide and methylamine. Up to 40% of the animals remained tumour-free. The other animals exhibited a greatly increased mean survival time. The post-challenge sera showed no detectable amounts of antibodies against the tumour cells.
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Tobacco mosaic virus was methylated, using various concentrations of dimethylsulfate. The methylated virus sample with still intact particles was subjected to sequential analysis. The sites and the degree of methylation were determined in the tryptic peptides. Tyrosine 139 and cysteine 27 are more accessible to methylation than tyrosine 72, lysine 68 and tyrosine 2. A limited number of carboxyl groups was also methylated. The ability of methylated and original tobacco mosaic virus to initiate the formation of humoral antibodies and the capacity to induce a delayed-type hypersensitivity reaction were investigated in STU mice. Original tobacco mosaic virus could not induce a delayed-type hypersensitivity reaction but methylated tobacco mosaic virus induced a delayed-type reaction, not depending on whether the virus particles were intact or disintegrated. This phenomenon was strictly linked with the presence of methylester groups.
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Red deer myoglobin has been fragmented by restricted tryptic digestion and by treatment with cyanogen bromide. The fragments have been separated by gel permeation. The core peptide derived from cyanogen bromide cleavage have been further digested with trypsin and the resulting peptides have been separated on Dowex 1X2. All fragments have been characterized by their amino acid composition, by determination of their N-terminal sequence using automatic Edman degradation and of their C-terminal sequence following the kinetics of amino acid cleavage by carboxypeptidases A and B. The complete sequence has been found to be identical with the already known sequence of sheep myoglobin except for residue 145 which is Gln in red deer globin and Glu in sheep globin. Reinvestigation of the corresponding sequence in sheep globin has shown that residue 145 of sheep globin is also Gln.
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