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Biomedical subjects

M Kern

Publications and source records attributed to M Kern.

At least 199 records · Page 11Linked to original sources
PubMed1972

Synthesis and secretion of gammaglobulin by lymph node cells: the acquisition of carbohydrate residues of immunoglobulin in relation to interchain disulfide bond formation (heavy and light chains-murine myeloma-mannose-glucosamine-galactose).

Acquisition of carbohydrates in the disulfide-linked heavy (H) and light (L) chain molecules of murine myeloma (ADJPC5), i.e., HH, HHL, and LHHL, was investigated. That some mannose and glucosamine residues are acquired by immunoglobulin precursor molecules was demonstrated by the detection of glucosamine and mannose in HH, HHL, and LHHL. In contrast, galactose was observed solely in LHHL molecules, which have an identical electrophoretic mobility to the secreted product. Furthermore, as judged from cells incubated with [(3)H]leucine, the more juvenile molecules HH and HHL were predominant in the rough microsome fraction, whereas LHHL was the principal molecular species in the smooth microsome fraction. Findings of this type were not observed in rabbit lymph node cells. Thus, galactose, as well as mannose and glucosamine, were found in the more juvenile molecule known for this species (HL). Moreover, the ratio of HL:LHHL, as judged from cells incubated with [(3)H]leucine, was about the same in rough and smooth microsomes.

Animals↗
PubMed1970

Synthesis and secretion of gamma-globulin by lymph node cells, VIII. Order of synthesis of the interchain disulfide linkages of immunoglobulins.

Murine myeloma cells (ADJ-PC-5), incubated in vitro with (3)H-leucine, secrete (3)H-immunoglobulin G as a single molecular species as judged by the migration characteristics of the labeled product on sodium dodecyl sulfateacrylamide gel electrophoresis. However, the fact that some of the interchain disulfide linkages of intracellular immunoglobulins had not been acquired permitted the identification of the following intracellular species: LHHL (identical to immunoglobulin G), HHL, HH, and L (H and L refer to heavy and light polypeptide chains, respectively). Although HH and HHL were readily observed, radioactivity was not detected in the region of the gel where HL would be expected. The time course for the appearance of the intermediates indicates that in these cells the first interchain disulfide bond to be formed occurs between heavy chains. In contrast, the interchain disulfide bonds of immunoglobulins derived from rabbit lymph node cells were acquired in a different order. The principal intracellular species observed were LHHL and HL, whereas HHL and HH were not detectable. These findings indicate that in this species the first interchain disulfide bond to be formed is that between the heavy and light chains of immunoglobulin G.

Animals↗