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Biomedical subjects

G Walter

Publications and source records attributed to G Walter.

At least 145 records · Page 8Linked to original sources
PubMed1991

Studies on human porin. VI. Production and characterization of eight monoclonal mouse antibodies against the human VDAC "Porin 31HL" and their application for histotopological studies in human skeletal muscle.

We report on the production and characterization of eight monoclonal mouse antibodies against the complete human VDAC "Porin 31HL". The antigen used was purified from a total membrane preparation of the transformed human B-lymphocyte cell line H2LCL. In Western blots all eight mAbs react with a single 31-kDa band in solubilized H2LCL membrane preparations thus demonstrating their specificity for the human VDAC "Porin 31HL". Concerning the epitope specificity we show that all eight mAbs equally react with the N-terminal part of human porin. Moreover, we demonstrate the expression of VDAC in the sarcolemma by indirect immunoenzyme labelling of cryosections of human skeletal muscle applying four of our mAbs. These data support our recent observations on the expression of porin channels in the plasmalemma of different normal and transformed human cell lines. VDAC in the plasmalemma is discussed as the molecular basis of the Blatz and Magleby channel.

Animals↗
PubMed1991

The naming of our species: appellations for the psychiatrist.

A number of appellations for the psychiatrist are discussed from a historical semantic and political perspective. Many are ambiguous, which may reflect an ambivalent attitude towards those who manage mental illness. The current designations, "headshrinker", "shrink" and "trick-cyclist" have considerable scope for interpretation. The expression "psycho, the rapist" may signify a disturbing "postambivalent" linguistic stage. The profession's potential responses to this development are considered.

Humans↗
PubMed1991

[Studies on human porin. V. The expression of "porin31HL" in the plasmalemma is not by cell transformation].

In recent papers we proved "Porin 31HL" to be located on the surface of human, EBV-transformed B lymphocytes. Here we present proof of "Porin 31HL" in the plasmalemma of normal human blood lymphocytes. For this purpose B and T lymphocytes were isolated from human heparinized blood and examined by indirect immunofluorescence techniques using different monoclonal antibodies against purified "Porin 31HL" and some B and T cell markers, respectively. For comparison a number of established cell lines of different origin were employed. Hence it followed that normal B and T cells as well as transformed and leukemic cells express "Porin 31HL" in their membrane. No significant quantitative differences could be seen. Consequently, the location of "Porin 31HL" in the plasmalemma is not a product of transformation.

Animals↗
PubMed1990

Association of protein phosphatase 2A with polyoma virus medium tumor antigen.

The polyoma virus medium and small tumor antigens, as well as simian virus 40 small tumor antigen, form specific complexes with two cellular proteins designated 61- and 37-kDa proteins. In this report, we demonstrate that the 61- and 37-kDa proteins correspond to the A and C subunits, respectively, of the serine- and threonine-specific protein phosphatase 2A (PP2A). On the one hand, antibodies raised against the 61-kDa protein reacted specifically with the purified A subunit of PP2A. Furthermore, the amino acid sequences of seven tryptic peptides from the A subunit were almost identical to sequences of the 61-kDa protein as deduced from the corresponding cDNA sequence. On the other hand, antibodies against the purified C subunit (catalytic subunit) of PP2A reacted specifically with the medium tumor antigen-associated 37-kDa protein. These data suggest a role of PP2A in cell transformation by polyoma virus and simian virus 40.

Adenoviruses, Human↗
PubMed1990

Physiochemical features of monoclonal idiotype-anti-idiotype complexes: importance of inter-chain disulfides for size distribution patterns and molecular geometries.

Cyclic tetramers represent the preferentially formed complexes of a murine monoclonal idiotype-anti-idiotype (Id-anti-Id) system consisting of IgG antibodies or (Fab')2 fragments at micromolar concentrations. The cleavage of inter-chain disulfides of both Id and anti-Id caused the predominant generation of cyclic dimers at the expense of larger aggregates, suggesting with regard to already published data that the hinge located interheavy-chain disulfides are essential for the strain.

Antibodies, Anti-Idiotypic↗
PubMed1990

Development of monoclonal antibodies for therapeutic drug monitoring.

For the development of multilayer fluorescent immunoassays to determine directly a variety of therapeutic drugs high specific monoclonal antibodies against the anticonvulsants carbamazepine, phenobarbital, phenytoin and valproic acid have been prepared. For each antibody a standard curve could be established showing good linearity and a suitable sensitivity scope. To validate the eligibility of the desired antibodies a variety of drugs and metabolites sharing structural similarities to the individual drugs were tested for their cross-reactivity. It could be shown that only a few very closely related compounds exhibited substantial cross-reactivity. These monoclonal antibodies are therefore assumed to be suitable for a TDM-assay development.

Antibodies, Monoclonal↗
PubMed1989

Evolutionary expression of the neuronal form of the src protein in the brain.

The protooncogene src encodes two proteins, designated pp60c-src+ and pp60c-src.pp60c-src+ is expressed only in neurons, whereas pp60c-src is expressed in neuronal and nonneuronal cells. pp60c-src+ differs from pp60c-src in that it contains an insert of 6 amino acids. To study the evolutionary conservation of the 6-amino acid insert, the expression of pp60c-src+ in the brain of animals from different classes was assayed by using pp60c-src+-specific antibodies raised against a synthetic peptide corresponding to the insert. pp60c-src+ was detected only in the brain of mammals, birds, and reptiles, but not amphibians and fish, whereas pp60c-src was present in the brain of all animals tested, including lobster (invertebrate). These findings indicate that pp60c-src+ may play a role in events associated with higher brain function, such as neuronal plasticity.

Amino Acid Sequence↗
PubMed1989

Molecular cloning and sequence of cDNA encoding polyoma medium tumor antigen-associated 61-kDa protein.

Polyoma virus medium tumor antigen forms specific complexes with several cellular proteins; among these is a protein of approximately 61 kDa. With antibodies directed against medium tumor antigen, the 61-kDa protein was purified from human 293 cells that were infected with a hybrid adenovirus and overexpressed medium tumor antigen. The purified 61-kDa protein was partially digested with protease V8, and one of the protease V8 fragments was isolated and partially sequenced. The amino acid sequence information was used to design mixed oligonucleotide probes for screening a cDNA library from human placenta. A clone was isolated that hybridized with two separate probes; the clone contained an insert with an open reading frame for 589 amino acids. By in vitro translation of the transcript from this insert, a protein was generated that had the same size and yielded the same pattern of protease V8 fragments as the original 61-kDa protein. Its amino acid sequence reveals 15 repeats, the majority of which are 39 amino acids long. This protein bears no resemblance to proteins in the data bank that was searched.

Amino Acid Sequence↗