Biomedical subjects

I G Haas

Publications and source records attributed to I G Haas.

22 records · Page 2Linked to original sources

PubMed1984

Immunoglobulin heavy chain toxicity in plasma cells is neutralized by fusion to pre-B cells.

A plasma cell hybridoma frequently loses its immunoglobulin heavy (H) chain spontaneously but rarely is production of its light (L) chain lost. Upon fusion to a pre-B-cell hybridoma that produces no Ig chain, the L chain is frequently lost. In cells without the L chain the H chain, which is derived from the plasma cell, is not chemically modified. Our results indicate that, in pre-B cells, but not in plasma cells, there must be a mechanism that neutralizes the toxic effect of free H chain.

Animals↗

PubMed1980

Effect of the aggregational state on the mitogenicity of lipoprotein from the outer membrane of Escherichia coli.

The effects of ultrasonication, electrodialysis, and centrifugation through sucrose gradients on the mitogenicity of the lipoprotein (LP) from the outer membrane of Escherichia coli were studied in several inbred mouse strains. LP is not readily soluble in aqueous solution. By ultrasonication for 1 minute we obtained LP aggregates which were fully mitogenic; prolonged sonification had no influence on activity. Solubilization in 4% sodium dodecyl sulphate (SDS) and centrifugation into sucrose gradients yielded different aggregation forms of LP, which were B-lymphocyte mitogens towards LPS non responder C3H/HeJ mouse splenocytes, and towards congenitally athymic nude mice. By electrodialysis, LP could be transformed into different salt forms. The TEA-salt of LP exhibited enhanced mitogenicity. The results suggest that the mitogenicity of lipoprotein is widely independent from the aggregational state in which it is offered to the cells.

Amino Acids↗

PubMed1980

Simultaneous expression of mouse immunoglobulins M and D is determined by the same homolog of chromosome 12.

A hamster-mouse hybrid cell line expressiong both murine IgM and murine IgD on the membrane was shown to have only one copy of mouse chromosome 12. This chromosome is known to carry the structural genes for the immunoglobulin heavy chains. Cloning of populations selected for loss of mouse membrane IgM yielded cells that had also lost expression of membrane IgD, but not the expression of hamster immunoglobulin heavy chain. Karyotype analysis of these subclones demonstrated the concurrent loss of the chromosome 12 present in the parental hybrid. Absence of this chromosome was confirmed by use of the isozyme acid phosphatase 1. The results of the genetic analysis prove that the coexpression of mu and delta immunoglobulin heavy chains is not due to long-lived immunoglobulin mRNA nor to the transcription of genes on homologous chromosomes. We conclude that the genetic information for IgM and IgD expressed by a single cell lies on the same chromosome.

Acid Phosphatase↗

PubMedDate not supplied

Immunoglobulin heavy chain binding protein.

Pre-B lymphocytes, and hybridomas derived from them, synthesize immunoglobulin heavy (IgH) chain in the absence of light (L) chain. In the Abelson virus transformed line 18-81, which is representative of the pre-B cell stage, we observed that at least some of the H-chains are bound to a protein other than L-chain. Here we show that the protein (which we term immunoglobulin heavy-chain binding protein, BiP) binds non-covalently to free IgH, but not to IgH associated with IgL.

Animals↗