Lentil-Lectin Affinity Chromatography of Surface Glycoproteins and the Receptor for IgE from Rat Basophilic Leukemia Cells

1979 ◽  
Vol 58 (1) ◽  
pp. 90-98 ◽  
Author(s):  
Ricki M. Helm ◽  
Daniel H. Conrad ◽  
Arnold Froese
Keyword(s):  
Affinity Chromatography ◽  
Leukemia Cells ◽  
Lectin Affinity Chromatography ◽  
Lectin Affinity ◽  
Lentil Lectin ◽  
Rat Basophilic Leukemia Cells ◽  
Basophilic Leukemia ◽  
Surface Glycoproteins

Ricin and lentil lectin-affinity chromatography reveals oligosaccharide heterogeneity of thyrotropin secreted by 12 human pituitary tumors

Metabolism ◽  
1992 ◽  
Vol 41 (9) ◽  
pp. 1009-1015 ◽  
Author(s):  
James Magner ◽  
Anne Klibanski ◽  
Henry Fein ◽  
Robert Smallridge ◽  
William Blackard ◽  
...  
Keyword(s):  
Affinity Chromatography ◽  
Pituitary Tumors ◽  
Lectin Affinity Chromatography ◽  
Human Pituitary ◽  
Lectin Affinity ◽  
Lentil Lectin

Serum thyrotropin (TSH) heterogeneity in euthyroid subjects and patients with subclinical hypothyroidism: the core fucose content of TSH-releasing hormone-released TSH is altered, but not the net charge of TSH

1995 ◽  
Vol 144 (3) ◽  
pp. 561-567 ◽  
Author(s):  
L Schaaf ◽  
J Trojan ◽  
T E Helton ◽  
K H Usadel ◽  
J A Magner
Keyword(s):  
Affinity Chromatography ◽  
Subclinical Hypothyroidism ◽  
Lectin Affinity Chromatography ◽  
Human Pituitary ◽  
Net Charge ◽  
Releasing Hormone ◽  
Lectin Affinity ◽  
The Core ◽  
Lentil Lectin ◽  
Fucose Content

Abstract The aims of the present study were to determine the influence of brief subclinical hypothyroidism on the isoforms of serum thyrotropin (TSH) and to examine the net charge of TSH in different metabolic states. Sera were obtained from euthyroid subjects (n=7) and from patients with subclinical hypothyroidism (n=8) before and 30 min after the intravenous administration of 200 μg thyrotropin-releasing hormone (TRH). The TSH from human pituitary extracts (IRP 68/38), basal and TRH-stimulated serum TSH was immunoconcentrated and further analysed by isoelectric focusing (IEF) and lentil lectin affinity chromatography. TSH immunoreactivity was determined in each specimen or fraction with an automated highly sensitive chemiluminometric TSH assay. We found that basal TSH in subclinical hypothyroidism, and TRH-released TSH in euthyroidism and in subclinical hypothyroidism is distributed in a similar neutral to acidic pattern, which significantly differs from the more alkaline to neutral isoform pattern of intrapituitary TSH (P<0·05). IEF analysis of pituitary standard TSH revealed 3 major peaks (pI values 7·5; 6·6; 5·8) whereas in most euthyroid or subclinically hypothyroid subjects 5 peaks were found. Lentil lectin affinity chromatography revealed that TRH-released TSH in euthyroid subjects has more core fucose residues than TSH from patients with subclinical hypothyroidism (64·6 ±6·7 vs 12·5 ±2·7%, P<0·0001). Thus pituitary standard TSH seems to be less mature material than circulating TSH. Perhaps no alteration in the IEF pattern of TSH was detected during early hypothyroidism because sialylation of TSH was increasing as sulfatation was decreasing. Nevertheless, a change in the core fucose content of TSH was detectable by lentil analysis. Journal of Endocrinology (1995) 144, 561–567

The distribution of antigen on the surface of RBL-2H3 rat basophilic leukemia cells observed by back-scattered electron imaging

1986 ◽  
Vol 44 ◽  
pp. 274-275
Author(s):  
R.F. Stump ◽  
J.R. Pfeiffer ◽  
JC. Seagrave ◽  
D. Huskisson ◽  
J.M. Oliver
Keyword(s):  
Cell Surface ◽  
Dynamic Properties ◽  
Leukemia Cells ◽  
Antigen Binding ◽  
Scattered Electron ◽  
Ige Receptor ◽  
Receptor Complexes ◽  
Rat Basophilic Leukemia Cells ◽  
Electron Imaging ◽  
Basophilic Leukemia

In RBL-2H3 rat basophilic leukemia cells, antigen binding to cell surface IgE-receptor complexes stimulates the release of inflammatory mediators and initiates a series of membrane and cytoskeletal events including a transformation of the cell surface from a microvillous to a lamellar topography. It is likely that dynamic properties of the IgE receptor contribute to the activation of these responses. Fewtrell and Metzger have established that limited crosslinking of IgE-receptor complexes is essential to trigger secretion. In addition, Baird and colleagues have reported that antigen binding causes a rapid immobilization of IgE-receptor complexes, and we have demonstrated an apparent increase with time in the affinity of IgE-receptor complexes for antigen.

Activation energy and lectin affinity chromatography of gamma-glutamyltransferase as a marker for enzyme heterogeneity

1989 ◽  
Vol 22 (2) ◽  
pp. 115-119 ◽  
Author(s):  
Joris R. Delanghe ◽  
Marc L. De Buyzere ◽  
Ivan K. de Scheerder ◽  
Uwe Faust ◽  
Roger J. Wieme
Keyword(s):  
Activation Energy ◽  
Affinity Chromatography ◽  
Lectin Affinity Chromatography ◽  
Gamma Glutamyltransferase ◽  
Lectin Affinity ◽  
Enzyme Heterogeneity
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