PubMed Health⌕ Search

Biomedical subjects

H Jaksche

Publications and source records attributed to H Jaksche.

5 recordsLinked to original sources
PubMed1991

Polyclonal anti-idiotypic antibodies mimicking the small cell lung carcinoma antigen cluster-5A interact with a panel of antibodies and induce specific immune response in animals.

Polyclonal anti-idiotypic antibodies (ab2) were generated by immunising goats with the murine IgG2a monoclonal antibody SWA20 which recognises the SCLC antigen cluster-5A, a tumour-associated sialoglycoprotein. Ab2 was shown to bind specifically to antibody SWA20, but not to isotype matched control antibodies. Pre-incubation with ab2 completely inhibited target cell binding of antibody SWA20 and of four other antibodies to cluster-5A antigen, while no effect was seen with antibodies to cluster-1 and cluster-w4 antigen. By these criteria the ab2 population consists of antibodies resembling in their reactivity pattern the cluster-5A antigen. Ab2 was used for immunisation of rabbits and two strains of mice; control animals received PBS or nonspecific goat IgG. Anti-anti-idiotype sera (ab3) were analysed in a series of radioimmunoassays for reactivity with goat IgG and reactivity with ab2. After blocking the nonspecific anti-goat response, ab3 could be shown to bind specifically to ab2 idiotype. As examined by an indirect cell ELISA with fixed cells, two out of six ab3 sera showed significantly higher binding ratios to antigen-positive SW2 cells as compared to antigen negative control cells. These findings indicate that the goat anti-SWA20 idiotype antibodies functionally represent the SCLC antigen cluster-5A and therefore may have potential for modulating the anti-tumour response through idiotypic network interactions.

Animals↗
PubMed1978

Human migration inhibitory factor: purification and immunochemical characterization.

Using gel filtration and preparative isotachophoresis, the migration inhibitory factor (MIF) was highly purified from human lymphocytes activated with concanavalin A. MIF is an acidic protein with a mol wt of approximately equal to 25,000 daltons as determined by gel filtration and analytical polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate. The protein inhibits migration of macrophages in the capillary test and in addition, has a slowing effect on the electrophoretic mobility of guinea pig peritoneal macrophages. Rabbit antibodies specific for this protein, as determined by immunochemical techniques, neutralized the biological effect of MIF on migration and on the electrophoretic mobility of macrophages.

Antigen-Antibody Reactions↗
PubMed1976

Escherichia coli enterotoxin: purification, partial characterization, and immunological observations.

Enterotoxin, a diarrhea-inducing protein elaborated by pathogenic Escherichia coli strains, was isolated from the supernate of fermenter cultures of E. coli strain P263, a porcine enteropathogen. Purification involved chromatography and preparative isotachophoresis. The resulting product appeared to be pure according to immunoelectrophoretic, disc electrophoretic, ultracentrifugal, and immunologic criteria. The enterotoxin had an apparent molecular weight of 102,000 daltons, and its isoelectric point was 6.90. The isolated product was active in inducing experimental diarrhea in adult rabbits and piglets. In small dosage it also elicited a drastic increase in adenylate cyclase activity in broken-cell preparations of cat heart tissue. The enterotoxin activity was acid labile and was destroyed by heat (65 C for 30 min). It is suggested that the heat-stable enterotoxin was derived from heat-labile enterotoxin by complexing with endotoxin or with capsular material in the culture supernatant. The antigenic relations between the heat-labile enterotoxins of enteropathogenic E. coli strains of different serological types and different host adaptations, as well as between the E. coli enterotoxin and that of Vibrio cholerae, were investigated.

Animals↗
PubMedDate not supplied

[Surgical treatment of fronto-maxillary tumors].

Surgical treatment of fronto-maxillary tumors requires interdisciplinary cooperation of maxillofacial surgeons and neurosurgeons. Depending on the site and extension of the tumor, it may be necessary to resort to generous excision of the frontal, temporal, sphenoid, zygomatic bones, orbita and nasal bone, including their soft-tissue covers; possibly even exenteration of the orbita and excision of dura are required. Closure of open subarachnoid space is mandatory. Dural defects are supplied with periosteum or free fascial grafts. Calvarial defect are usually repaired with large rotation flaps of the scalp. In exceptional cases pedicled flaps from more remote areas or microsurgically vascularized grafts are used. The facial area is supplied either with flaps or split skin grafts, depending on the situation. Open paranasal sinuses must be drained via the nasal sinus. Remaining facial defects are treated prosthetically.

Adult↗