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Biomedical subjects

H J Hartmann

Publications and source records attributed to H J Hartmann.

At least 37 records · Page 2Linked to original sources
PubMed1990

Monoclonal antibodies to monomeric rat liver metallothionein-I: the immunoreactivity of lysine residues in metallothionein.

Regardless of the weak immunological response against the low-Mr metallothioneins (MTs) the production of murine monoclonal antibodies (mAbs) to monomeric rat liver MT-I was successful. ELISA revealed two groups of mAbs which exhibited different specificities as examined on the native and the lysine-residue modified antigen (Ag). One "lysine-directed mAb" group, consisting of three mAbs, exhibited a specific immunoreactivity with the lysine-containing epitopes of MTs. Their role in the antigenicity of MTs was examined by modifying these residues using glutaraldehyde (GA). Titration with GA resulted in a progressive decline in Ag recognition in the immunoblot; this was completely leveled off when equimolar concentrations were reached. A similar response employing the GA-modified protein in the ELISA was noticed. The second group of mAb cross-reacted with various MTs of different origin, indicating that the common, lysine-free NH2-terminus is exclusively recognized. In direct ELISA of cross-linked MTs, the observed reactivities were much more pronounced. Iodoacetamide (IA) modification of the lysines confirmed the above observations of the GA-derived Ag. Notably, the immunoreactivity was not affected when the cysteine residues were IA-carboxymethylated, nor did the subsequent loss of metals diminish the immunological response in the immunoblot.

Animals↗
PubMed1990

Rapid quantification of planktonic ciliates: comparison of improved live counting with other methods.

THE FOLLOWING EFFICIENT AND QUANTITATIVELY VALID METHOD TO FILTER CONCENTRATE AND COUNT LIVE PLANKTONIC CILIATES WAS DEVELOPED AND COMPARED WITH OTHER TREATMENTS: unconcentrated (raw) samples and centrifuged samples were counted live, and the effects of five different fixatives (HgCl(2), Lugol's iodine, formaldehyde, glutaraldehyde, and Champy-DaFano) on the counts were monitored. Samples originated from a eutrophic mountain lake (Lake Aydat, near Clermont-Ferrand, France). Overall, live filtered counts were similar to counts of raw samples, but they were significantly higher (2 to 2.3 fold, P < 0.05) by analysis of variance than counts from centrifuged samples. Nevertheless, some taxa, i.e., Halteria and Loxodes spp., were sensitive to filtration. The live filtered counts were also comparable to counts of raw HgCl(2)-fixed and settled samples. HgCl(2) and Lugol fixation consistently gave the highest total counts, while significantly lower counts were always obtained with Champy-DaFano-fixed samples. Losses due to fixation were insignificant for raw samples but were substantial and statistically significant in concentrated samples (15% after filtration and 71% after centrifugation, compared with counts from the corresponding live samples). Live counting of passively filter-concentrated ciliates has many advantages over other methods. It is two to four times quicker and more efficient. Ciliates are recognized with certainty, more species are identified, and enumeration of dead organisms (e.g., tintinnid loricas) is avoided. It should be recommended as a quantitatively valid alternative to classical methods for assessing planktonic ciliate populations.

Journal Article↗
PubMed1990

[Replantation].

Explore the source record for details and available documents.

Humans↗
PubMed1989

Copper-thionein in melanoma.

The phenomenon of an elevated copper concentration in melanoma tumors was examined. It was demonstrated that 50-60% of total tissue copper is associated with metallothionein. The amino acid composition, electronic absorption and fluorescence were identical to that of the many known vertebrate Cu-thioneins. The immunological identification of melanoma tissue metallothionein was successful. The elevated Cu-thionein concentration in melanoma tumor tissue is not yet understood. It appears to be a common concept that in most tumors transient changes of the copper status parallel the metallothionein levels.

Amino Acids↗
PubMed1989

Copper-thionein in leucocytes.

Upon incubation of peripheral leucocytes with copper sulphate a dramatic cellular copper uptake reaching levels of 25-50-fold compared to that of the natural copper content was measured. The orange-red fluorescence of the copper-treated white blood cells was assigned to the formation of Cu(I)-thiolate clusters in Cu(I)-thionein. A protein of 6-8 kDa was isolated from homogenized bovine leucocytes and characterized by its electronic absorption and amino acid composition to be identical to the above Cu(I)-thionein. More than 70% of the intracellular copper was attributed to this protein in its monomeric and polymeric form. Cu-thionein formation was more pronounced in monocytes than in granulocytes. As most intriguing phenomenon, the release of this Cu-thionein from leucocytes, was also noticed. The occurrence of Cu-thionein in leucocytes and the excretion of the intact Cu(I)-thiolate protein is of considerable interest with respect to the observed elevated copper levels in white blood cells and plasma during tumor malignancies and inflammatory processes.

Amino Acids↗
PubMed1989

Cu(I)-thionein release from copper-loaded yeast cells.

The release of intact Cu(I)8-thionein from copper-resistant copper-loaded yeast cells, strain X2180-1Aa, has been shown. This copper(I)-thiolate-rich protein was characterized and compared with the chemical and physiocochemical properties of intracellular yeast Cu-thionein. The same molecular mass and stoichiometry of 8 mol copper atoms/mol protein was found. No detectable difference between the Cu-thioneins was seen in luminescence emission, electronic absorption in the ultraviolet region, chiroptical data or amino acid composition. The importance of stable Cu(I)-thiolates in Cu-thionein as a safe vehicle for transporting copper in a non-reactive manner is confirmed.

Carrier Proteins↗
PubMed1989

[Therapy possibilities in threatened failure of implants].

Parodontological and mucogingival treatment are very successful in case of a prognosed failure of implants. If however they are in vain, the bony defect can be filled up with hydroxylapatit (HA). You must apply HA with great care well aware that there are hardly any long term success described. Future will prove the osseointegration and indulgence of HA in the bone.

Dental Implantation, Endosseous↗
PubMed1989

[Reduction of bony periodontal pockets with hydroxyapatite].

If you can't reduce a periodontal bone defect of more than 6 mm with a conservative therapy you can open up the pocket with a marginal incision. The granulation tissue must be removed carefully, open up the surrounding spongiosa and clean the tooth from calculus. HA-Granula is filled into the pocket but don't overfill it. Use Matrix-sutures to sew the wound very dense against saliva. A final splint stabilizes the tooth.

Alveolar Process↗
PubMed1988

Differently bound copper(I) in yeast Cu8-thionein.

The reactivity of yeast Cu-thionein in the presence of the Cu(I)-chelators, bathocuproinesulphonate and cuproine, was examined to distinguish between possible differently coordinated Cu(I). Electronic absorption measurements revealed that two out of eight coppers of the protein reacted within seconds with the chelator. At the same time, the shape and magnitude of the characteristic Cotton bands attributable to the Cu(I)-thiolate chromophores remained constant. Due to the successful removal of circular dichroic silent copper, all specific theta Cu values rose by 53% of the original value. Thus, it is strongly suggested that two or more distinct types of Cu(I) ought to be present in Cu8-thionein. In the light of the many different Cu/cysteine ratios of Cu-thioneins from vertebrate and microbial origin, possible interconversion reactions of the Cu(I)-thiolate centres seem to be likely.

Carrier Proteins↗
PubMed1986

Copper transport from Cu(I)-thionein into apo-caeruloplasmin mediated by activated leucocytes.

A study on the transfer of copper from Cu-thionein into apo-caeruloplasmin, using Cu-thionein that was previously oxidised by activated leucocytes, was performed. Cu(I)-thiolate oxidation was conveniently monitored by the progressive decline of the specific Cotton bands between 400 and 300 nm. The characteristic e.p.r. properties and NN-dimethyl-p-phenylenediamine oxidase activity indicated a successful formation of caeruloplasmin. Taking into account the simultaneous occurrence of leucocytes, apo-caeruloplasmin and Cu-thionein in blood plasma, such an interaction would favour a possible metabolic link between either copper protein.

Animals↗