1977
DOI: 10.1016/0092-8674(77)90101-5
|View full text |Cite
|
Sign up to set email alerts
|

Abnormalities in the glycosylation of immunoglobulin heavy chain and an H-2 transplantation antigen in a mouse myeloma mutant

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2
1
1

Citation Types

0
13
0

Year Published

1978
1978
1984
1984

Publication Types

Select...
9

Relationship

0
9

Authors

Journals

citations
Cited by 15 publications
(13 citation statements)
references
References 27 publications
0
13
0
Order By: Relevance
“…Immunoglobulin production was found in the cell lines LAZ 135 and LAZ 165. In contrast, the remaining four cell lines, LAZ 153, LAZ 184, LAZ 202, and S-2, failed to produce immunoglobulin detectable by this technique (Table VIII) (42,43). Cell lines derived from two patients, LAZ 135 and LAZ 165, had immune characteristics that were indistinguishable from LCL derived from normal individuals.…”
Section: Introductionmentioning
confidence: 93%
“…Immunoglobulin production was found in the cell lines LAZ 135 and LAZ 165. In contrast, the remaining four cell lines, LAZ 153, LAZ 184, LAZ 202, and S-2, failed to produce immunoglobulin detectable by this technique (Table VIII) (42,43). Cell lines derived from two patients, LAZ 135 and LAZ 165, had immune characteristics that were indistinguishable from LCL derived from normal individuals.…”
Section: Introductionmentioning
confidence: 93%
“…We have found galactosamine in both//chain disease proteins which were studied in our laboratory (Mihaesco et al 1976, Mihaesco & Miglierina, unpublished results) and the unexpected presence of galactosamine has also been noted in three y chain disease proteins (Clamp & Johnson 1972, Garver et al 1977. It is worth noting than abnormal glycosylation was found in a mouse myeloma mutant with short heavy chains (Weitzman et al 1977).…”
Section: Structural and Cellular Studiesmentioning
confidence: 99%
“…Glycosylation defects that block insertion of the Thy-I protein and also affect glycosylation of other cell surface components have been reported by Trowbridge et al (19). In a study of the abnormal glycosylation of immunoglobulin heavy chain in a myeloma mutant, Weitzman et al (20) found abnormal glycosylation of the H-2D but not the H-2K product of the mouse major histocompatibility locus. Because the morphologic and adherence properties of the variants were so different from those of J774, the defect(s) may involve general membrane processing steps.…”
mentioning
confidence: 93%