PubMed Health⌕ Search

Biomedical subjects

A Dautigny

Publications and source records attributed to A Dautigny.

54 records · Page 3Linked to original sources
PubMed1983

Cell-free synthesis of hemocyanin from the scorpion Androctonus australis. Characterization of the translation products by monospecific antisera.

Translation of Androctonus australis poly(A)-RNA in vitro led to a number of polypeptides products (8-10) of 70-73 kDa analyzed by two-dimensional gel electrophoresis and identified by immunoprecipitation with an anti-(dissociated hemocyanin) antiserum. The translated hemocyanin polypeptides have the same physico-chemical characteristics as authentic hemocyanin subunits. Subunits Aa 2 and Aa 4 have been identified with monospecific antisera characterized (a) by their capability of reacting with their homologous subunit and (b) by their inability of binding to cross-reacting subunits. Each polypeptide chain is coded by a different messenger without significant post-translational events. Hemocyanin could be detected among the translation products of the poly(A)-RNA isolated from the cuticle under the carapace.

Animals↗
PubMed1980

Characterization of alpha 1-microglobulin in human colostrum and milk.

The mean concentration of alpha 1-microglobulin in human colostrum and milk, estimated by electroimmunoassay, was found to be about 0.4-0.6 mg/l and 0.1-0.2 mg/l, respectively. Both liquids contained alpha 1-microglobulin in mono- and dimeric forms, while the presence of higher polymeric forms, as characterized in plasma, could not be demonstrated.

Alpha-Globulins↗
PubMed1980

alpha 1-Microglobulin from normal and pathological urines.

alpha 1-Microglobulin was purified from normal and pathological urines. Significant differences were found in the amino acid compositions of the alpha 1-microglobulin isolated from these two sources. In addition electrofocusing of alpha 1-microglobulin from normal urine gave rise to two peaks of equal intensity with rather acidic isoelectric points (3.8 and 4.2), whilst alpha 1-microglobulin from pathological urine showed two peaks in a 1:5 ratio with less acidic isoelectric points (4.2 and 4.7). Further charge heterogeneity was also observed in the second peaks from both sources. The sugar compositions were also established, as well as the N-terminal sequences of the alpha 1-microglobulin of both peaks isolated from normal and pathological urines.

Alpha-Globulins↗
PubMed1979

Immunological and serological data concerning human histocompatibility antigens (HLA) and alpha 1-microglobulin co-purified from urine.

Serologically active glycoproteins (HLA) purified from urine contained only about 4% HLA antigens co-purified with alpha 1-microglobulin. The immunization of rabbits with the serologically active product gave rise to an antiserum containing two kinds of antibodies: anti-HLA-A9 and anti-alpha 1-microglobulin. The anti-HLA-A9 antibodies were detected by the lymphocytotoxicity and indirect immunofluorescence techniques against peripheral blood lymphocytes and cultured lymphoid cell lines. Anti-alpha 1-microblobulin antibodies were detected by immunoprecipitation in gel. Pure alpha 1-microglobulin gave rise to an antiserum directed only against alpha 1-microglobulin. This antiserum did not react with peripheral blood lymphocytes and cultured lymphoid cell lines.

Alpha-Globulins↗
PubMed1978

Molecular data on urinary glycoproteins with human leucocyte antigen (HLA) activity.

Two glycoproteins characterized by their serological activities (HLA-A9 and HLA-B12), their isoelectric points and their molecular weights were purified from urine from a patient suffering from tubular proteinuria (cystinosis). Their physicochemical properties as well as an important increase of their specific activities during the different purification steps suggested that they behave as human leucocyte antigens (HLA) which had been excreted into urine. Their amino acid compositions and N-terminal sequences were different to those described for HLA solubilized from cultured human lymphoblast cell lines. The N-terminal sequences of the two serologically active glycoproteins were identical to the N-terminal sequence of another recently purified human urinary glycoprotein called human complex-forming glycoprotein. The relationship between HLA, human complex-forming glycoprotein and the serologically active urinary glycoproteins is discussed.

Amino Acid Sequence↗
PubMed1977

[Molecular aspects of 2 human urinary glycoproteins with histocompatibility antigen (HLA) serological activity].

Two serologically active urinary glycoproteins (HLA-A 9 and HLA-B 12) were isolated from urine provided by a patient suffering from tubular proteinuria. Their N-terminal sequences were automatically determined. The latter were identical with the sequence of another urinary glycoprotein (protein HC). The relationship between protein HC and the serological activity is discussed.

Amino Acid Sequence↗
PubMed1975

Human platelets as a source of HL-A antigens : a study of various solubilization techniques.

The efficiency of various methods of solubilizing HL-A platelet antigens was investigated. The yield of soluble material was compared with that obtained from lymphocytes in culture in order to judge the quality of platelets as a source of HL-A antigens. The conclusion was reached that platelets, easily obtainable, can be considered as a good source of HL-A antigens.

Blood Platelets↗
PubMed1975

A molecular defect in thrombasthenic platelets.

An IgG antibody found in the serum of a thrombasthenic patient reacted in complement fixation with platelets from 350 normal individuals but was nonreactive with platelets from eight other thrombasthenic patients. ADP-induced aggregation of normal platelets was inhibited by the patient's antibody. Family studies using the quantitative complement fixation test showed that healthy heterozygotes were easily distinguishable from normal or thrombasthenic individuals since their platelets had an intermediate amount of the reactive antigen. Indirect immunoprecipitation tests using this serum and soluble membrane antigens labeled with iodine-125 that had been extracted from normal platelets by the detergent Nonidet P-40 gave a single radioactive peak at 120,000 mol wt in sodium dodecyl sulfate polyacrylamide gel electrophoresis. A similar estimate of the molecular weight was obtained from Sephadex G-200 filtration of the soluble antigens extracted from normal platelets by spontaneous release or chaotropic agents and tested in complement fixation with the patient's serum. These findings strongly suggest that the molecule recognized by this antibody is absent or structurally modified in thrombasthenia cases and that it may be involved in platelet aggregation.

Adenosine Diphosphate↗
PubMed1975

Spontaneous release of soluble HL-A antigens from platelets during conservation.

Experiments with the aim of studying the solubilisation of HL-A antigens from blood platelets by methods which do not involve any biologically active processes (moderate, discontinuous agitation of a low concentration of platelets suspended in a saline medium, in the presence of an antiseptic; supernatants collected at frequent intervals) have shown that platelets release membrane proteins, including HL-A antigens, spontaneously. Optimal conditions for the treatment of membrane proteins have been perfected. The great stability of HL-A antigens under these conditions permits prolonged treatment. The products extracted are soluble and extremely complex. The molecular weight of the HL-A antigens is between 40,000 and 70,000.

Blood Platelets↗
PubMedDate not supplied

The structural gene coding for myelin-associated proteolipid protein is mutated in jimpy mice.

Mutations affecting developmental processes may allow some insight into the complexity of the biological processes involved. In mice, two mutants that affect myelin formation in the central nervous system, jimpy and shiverer, have proved to be useful models for the study of this process. The predominant proteins in myelin are the major myelin proteolipid (PLP) and the myelin basic proteins (MBP), which together account for 80-90% of total myelin proteins. It has recently been shown that the shiverer mutation is located in the MBP structural gene, but the site of the jimpy mutation, which is X-chromosome-linked and may be similar to the sex-linked dismyelinization human disease, Pelizaeus-Merzbacher disease, remains unclear. Here we provide evidence, based on a combined genetic and biochemical approach, that the sex-linked recessive mutation jimpy is located in the structural gene coding for PLP.

Animals↗