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M L Egan

Publications and source records attributed to M L Egan.

35 records · Page 2Linked to original sources
PubMed1978

Amino-terminal sequence of a carcinoembryonic antigen-like glycoprotein isolated from the colonic lavages of healthy individuals.

A glycoprotein has been isolated from the colonic lavages of healthy individuals that is immunologically equivalent to carcinoembryonic antigen purified from tumor tissue. The NH2-terminal sequence of the glycoprotein from normal colon lavages is Lys-Leu-Thr-lle-Glu-Ser-Thr-Pro-Phe-(Asn)-Val-Ala-Glu-Gly-Lys-Glu-Val-(Leu,lle)-(Leu,lle)-(Leu,lle)-Val-(His,Arg?)-?-(Leu,lle). This is homologous to the NH2-terminal sequence of 23 of the first 24 amino acids of carcinoembryonic antigen isolated from tumor tissue.

Amino Acid Sequence↗
PubMed1977

Detection of circulating tumor antigens.

A wide variety of malignancies have associated tumor antigens. Two which have proven useful in the clinical detection and management of cancer are alphafetoprotein (AFP) and the carcinoembryonic antigen (CEA). These materials have been determined both by radioimmunoassay and by a newer technique employing enzymes to replace radioisotopea as markers. The interpretation of these immune assay results and the factors governing the shape of the standard curve are discussed. The advantages of 57Co over 22Na as a volume marker in radioimmunoassay are presented.

Animals↗
PubMed1977

Management training for public welfare agencies: why the need remains unmet.

This paper presents findings from a 1976 survey of public welfare agencies' offices of staff development and training. These offices primarily provide program-specific training directly related to agencies' ongoing programs. Although they recognize broader managerial training as an important unmet need, they do not feel they have the in-house expertise or free resources to provide it. At the same time, they are prevented from purchasing it outside the agency by its high cost. This need will remain unmet unless substantial federal financial subsidies are provided.

Administrative Personnel↗
PubMed1977

Isolation and immunochemical and chemical characterization of carcinoembryonic antigen-like substances in colon lavages of healthy individuals.

Material with carcinoembryonic antigen (CEA)-like activity, isolated from colon lavages of healthy individuals, has been chemically characterized. The CEA-like activity in these lavages was purified by gel filtration on Sepharose 6B and Sephadex G-200 and by affinity chromatography on concanavalin A linked to Sepharose. The purified material migrated in polyacrylamide-sodium dodecyl sulfate electrophoresis as a single diffuse band with mobility identical with that of tumor CEA. The material with CEA activity from tumor tissue and from normal colon lavages gave lines of identity in double diffusion experiments and had similar inhibition curves with esssentially the same specific activities in a radioimmune assay for tumor CEA. The amino acid and carbohydrate compositions were similar to that observed for CEA tumor preparations. Lysine was the single amino terminus. Methylation analysis demonstrated that the monosaccharide linkages were similar to those in CEA isolated from tumor tissue.

Adult↗
PubMed1976

Physical characterization and structural studies of the carcinoembryonic antigen.

Knowledge of the structure of carcinoembryonic antigen (CEA) is essential if we are to understand the relationship of this molecule to similar, possibly cross-reacting, molecules present in nonmalignant states. Electron microscopy shows that at neutral pH, CEA particles consist of homogeneous, morphologically distinctive, twisted rod-shaped particles, about 9 X 40 nm. The carbohydrate structure of CEA has been studied by periodate oxidation. All the N-acetylneuraminic acid and fucose and a portion of the galactose and mannose were destroyed by the first periodate treatment without altering immunological activity. N-Acetylneuraminic acid was shown to be linked to galactose since its prior removal with neuraminidase led to an equivalent increased destruction of galactose by one treatment with periodate. Significantly, even after 100% of the fucose and N-acetylneuraminic acid, 75% of the galactose, and 50% of the N-acetylglucosamine and mannose were destroyed by serial periodate oxidation (Smith degradation), the remaining portion of the CEA molecule lost no more antigenic activity than did control samples where periodate was omitted. No carbohydrate was lost or destroyed in the control reaction.

Carbohydrates↗
PubMed1975

The chemistry of carcinoembryonic antigen.

The structure of carcinoembryonic antigen is being determined as an approach to greater diagnostic specificity in the radioimmune assay. Examination by combined gas chromatography-mass spectrometry of derivatized saccharides from CEA has given a general outline of its carbohydrate structure. Sialic acid and fucose were completely destroyed, and galactose and mannose were partially destroyed by a single periodate treatment. Serial periodate oxidation (Smith degradation) destroyed additional amounts of galactose and mannose, as well as significant amounts of N-acetylglucosamine. Antigenic activity persisted, indicating that the residues destroyed played little, if any, part in the antigenicity of DEA.

Animals↗
PubMed1975

The binding of carcinoembryonic antigen by antibody and its fragments.

In order to assess the potency of antigenic fragments of carcinoembryonic antigen (CEA) in the radioimmune assay; it is necessary to know whether the high affinity of goat anti-CEA antibody (which makes possible the detection of as little as 10--11M CEA) is due to bivalent binding of the CEA molecule. Immunoglobulin G and the F(ab')2 and Fab fragments derived from it were prepared from an anti-CEA serum and tested for their abioity to bind CEA. Equivalent concentrations of binding sites of the bivalent F(ab)2 and univalent Fab fragments of anti-CEA were identical to the immunoglobulin G fraction in the standard inhibition curve. Fragments of CEA obtained by trypsin digestion produced equivalent inhigition curves when tested with either immunoglobulin G, F(ab')2, or Fab". This, increased avidity due to bivalent binding to a single antigen molecule cannot be invoked to explain the sensitivity observed in the CEA assay. This high sensitivity implicates the protein rather than the carbohydrate as an important part of the antigenic determinant(s) of CEA.

Animals↗
PubMedDate not supplied

Immunochemical characterization of the polysaccharide antigens of group B streptococci.

Mouse monoclonal antibodies were used in the immunochemical characterization of the polysaccharide antigens of group B streptococci (GBS). Monoclonal antibodies specific for the sialylated form of the GBS type III polysaccharide were highly protective in a mouse model of GBS type III infection, whether of IgM, IgG2a, or IgA isotypes, but monoclonal antibodies specific for the nonsialylated form of the type III antigen were not protective, regardless of isotype. Monoclonal antibodies reacting with the type II polysaccharide antigen could be divided into two general antigen binding groups on the basis of the ability of beta-methylgalactopyranoside to inhibit their binding to purified type II antigen. Various proportions of antibodies with the two specificities were observed in rabbit and human sera. Although it was previously reported that rabbit antisera could not distinguish between the sialylated and nonsialylated forms of the type Ib polysaccharide, mouse monoclonal antibodies were found to exhibit exclusive specificity for one or the other form of the antigen. Only monoclonal antibodies specific for the sialylated Ib polysaccharide were protective in a mouse model.

Animals↗