Lectin Affinity Chromatography: An Efficient Method to Purify Horse IgG3

2020 ◽  
pp. 301-310
Author(s):  
Salvatore G. De-Simone ◽  
David W. Provance
Keyword(s):  
Affinity Chromatography ◽  
Efficient Method ◽  
Lectin Affinity Chromatography ◽  
Lectin Affinity

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

Isolation of a 32 kDa Mycobacterium tuberculosis protein by lectin affinity chromatography

1994 ◽  
Vol 108 (2) ◽  
pp. 265-272
Author(s):  
L.F. Montaño ◽  
F. Massó ◽  
A. Páez ◽  
S. Sandoval ◽  
L. Vázquez ◽  
...  
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Affinity Chromatography ◽  
Lectin Affinity Chromatography ◽  
Lectin Affinity

Transferrin glycosylation in hypoxia

1991 ◽  
Vol 69 (4) ◽  
pp. 239-244 ◽  
Author(s):  
Erwin Regoeczi ◽  
J. Michael Kay ◽  
Paul A. Chindemi ◽  
Ouahida Zaimi ◽  
Kaye L. Suyama
Keyword(s):  
Affinity Chromatography ◽  
Sea Level ◽  
Anion Exchange ◽  
Immunoglobulin G ◽  
Lectin Affinity Chromatography ◽  
Lectin Affinity ◽  
Hypobaric Chamber

The aim of this study was to examine the effect of reduced O2 tension on the glycosylation of transferrin. Rats were placed in a hypobaric chamber (380 mmHg) that corresponded to an altitude of 5486 m above sea level for 21 days. The animals responded with marked increases in hematocrit (from 44 to 76%) and cardiac weight, and with reductions in the concentration of plasma transferrin averaging 15%. Analyses of their plasma transferrin by serial anion-exchange and lectin affinity chromatography revealed no changes in the extent of glycan branching. However, there was a moderate rise in the proportion of fucosylated transferrin molecules (fucosylation index) and a slight decrease in the transferrin fraction bearing a tetrasialylated biantennary glycan. The fucosylation index correlated positively with plasma transferrin concentrations in the test animals, but not in the controls. In contradistinction to the situation with transferrin, hypoxic rats exhibited a reduced fucosylation index of immunoglobulin G.Key words: fucosylation index, hypoxia, immunoglobulin G, lectin affinity chromatography, transferrin.

Antibodies Against Platelet Membrane Glycoproteins: Effect On Ristocetin-Induced Platelet Aggregation

1981 ◽  
Author(s):  
E F Ali-Briggs ◽  
C S P Jenkins ◽  
K J Clemetson
Keyword(s):  
Platelet Aggregation ◽  
Affinity Chromatography ◽  
Platelet Membrane ◽  
Receptor Activity ◽  
Free Medium ◽  
Membrane Glycoproteins ◽  
Lectin Affinity Chromatography ◽  
Lectin Affinity ◽  
Fab Fragments ◽  
Induced Aggregation

Some membrane glycoproteins (GPs) have been isolated by lectin-affinity chromatography and antibodies towards them have been raised. Platelets that have lost glycocalicin no longer respond to ristocetin-human VIII:WF, bovine VIIIR:WF, or to anti-glycocalicin or anti-GPs la and lb antibodies but are still agglutinated by anti-GPs lib and Ilia antibodies. Anti-GPs la and lb and anti-glycocalicin antibodies, IgG and Fab' fragments inhibited ristocetin- human VIIIR:WF- and bovine VIIIR:WF-induced aggregation of fixed, washed platelets and of platelets in plasma while anti-GPs Hb and Ilia antibodies were without effect.Crossed immunoelectrophorectic studies showed that glycocalicin was present on whole platelets in only trace amounts; anti-glycocalicin antibodies, however, recognized a slower migrating component. Platelets incubated in an EDTA-free medium no longer respond to ristocetin-human VIIIRrWF. Membranes isolated from such platelets contained glycocalicin which cross-reacted with a remnant of the slower migrating component. Anti-GPs la and lb antibodies gave more complex patterns but it was possible to identify the slower moving component recognized by the anti-glycocalicin antibodies.These results show that glycocalicin is not normally found as such on whole platelets but is present as a precursor which is most likely GP lb. On degradation of this precursor, glycocalicin is released from the membrane and VIIIRrWF-receptor activity is lost.

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