Biomedical subjects

C Löffler

Publications and source records attributed to C Löffler.

22 records · Page 2Linked to original sources

PubMed1991

Mapping of the ribophorin II (RPN II) gene to human chromosome 20q12-q13.1 by in-situ hybridization.

Ribophorin I and II (RPN I and RPN II), two specific glycoproteins, span the rough regions of the endoplasmic reticulum (RER) and are thought to play an important role either in translocation or in the maintenance of RER. Studies with human-mouse somatic cell hybrids have localized the gene for RPN I on human chromosome 3q, while RPN II is on chromosome 20. Using a radioactive labelled cDNA probe, we have regionally mapped the RPN II gene to human chromosome 20q12-q13.1 by in situ hybridization. This assignment predicts a location of the murine homologue, Rpn-2, to the syntenic segment on mouse chromosome 2 in close proximity to Ada, Src and Gnas.

Chromosome Mapping↗

PubMed1991

The gene for the novel vasoactive peptide endothelin 3 (EDN3) is localized to human chromosome 20q13.2-qter.

Endothelin 3 is a novel vasoactive peptide of unique structure and belongs to the endothelin gene family. Though it mainly functions as a vasoconstrictor/pressor, it plays a major role in a wide variety of other biological functions, possibly as a novel neuropeptide. Studies with human-mouse somatic cell hybrids have suggested that the gene EDN3 is localized on human chromosome 20. We confirmed this localization and regionally mapped the gene to the region 20q13.2-q13.3.

Animals↗

PubMed1991

The gene for human growth hormone-releasing factor (GHRF) maps to or near chromosome 20p12.

Growth hormone-releasing factor (GHRF), a hypothalamic releasing factor also named somatocrinin, influences the secretion and synthesis of growth hormone. Human GHRF is encoded by a single gene which was assigned to chromosome 20 by dot-blot analysis of DNA from dual laser sorted chromosomes. Using a radioactive cDNA probe, we localized the GHRF gene to chromosome 20p12 or near band 20p12.

Chromosome Banding↗

PubMed1982

Human granulocyte elastase is inhibited by the urinary trypsin inhibitor.

Two forms of urinary trypsin inhibitor, A and B, were purified from the urine of pregnant women. Form A was the only inhibitor present in fresh urine and inhibitor B arose from degradation of A upon storage of urine. The molecular masses of A and B were about 44 and 20 kDa, respectively, as judged from dodecyl-sulfate polyacrylamide gel electrophoresis, but about 60 kDa and 30 kDa, respectively, as judged from gel filtration analysis. The discrepancy can perhaps be explained by the carbohydrate content amounting to about 10% of each inhibitor. After reduction with mercaptoethanol, inhibitor A and inhibitor B had identical apparent molecular masses of about 20 kDa on dodecyl-sulfate gel electrophoresis. These results and the results of amino acid analysis suggest that one molecule of inhibitor A yields two molecules of inhibitor B. On agarose gel electrophoresis inhibitor A migrated as a rather broad band in the prealbumin region and inhibitor B as 3 well defined bands in the beta-region. Specific antisera were raised against inhibitor A and B. The two inhibitors showed the immunologic reaction of identity with each other and with the plasma inter-alpha-trypsin inhibitor, when using either antiserum. The inhibitors both gave quantitative inhibition of bovine trypsin, the results indicating a 4/1 trypsin/inhibitor molar ratio for A and a 2/1 ratio for B. The two substances also effectively inhibited granulocyte elastase. No inhibition of porcine pancreatic elastase was demonstrable.

Amino Acids↗