Flow-cytometric analysis of peripheral blood lymphocytes in patients with chronic idiopathic neutropenia of adults

1997 ◽  
Vol 75 (3) ◽  
pp. 103-110 ◽  
Author(s):  
D. Kyriakou ◽  
H. A. Papadaki ◽  
D. Sakellariou ◽  
A. G. Eliopoulos ◽  
V. Kapsimali ◽  
...  
Keyword(s):  
Peripheral Blood ◽  
Flow Cytometric Analysis ◽  
Peripheral Blood Lymphocytes ◽  
Blood Lymphocytes ◽  
Flow Cytometric ◽  
Chronic Idiopathic Neutropenia

Flow Cytometric Screening for the HLA ‐B27 Antigen on Peripheral Blood Lymphocytes

2005 ◽  
Vol 33 (1) ◽  
Author(s):  
Wilfried H.B.M. Levering ◽  
Kees Sintnicolaas ◽  
Henk Wind ◽  
Herbert Hooijkaas ◽  
Jan W. Gratama
Keyword(s):  
Peripheral Blood ◽  
Peripheral Blood Lymphocytes ◽  
Hla B27 ◽  
Blood Lymphocytes ◽  
Flow Cytometric

scholarly journals Flow cytometric analysis of lectin binding to human peripheral blood lymphocytes

1982 ◽  
Vol 208 (1) ◽  
pp. 69-75 ◽  
Author(s):  
G Blackledge ◽  
B Vose ◽  
A J Morris ◽  
D Crowther ◽  
J T Gallagher
Keyword(s):  
Concanavalin A ◽  
Peripheral Blood ◽  
Human Peripheral Blood ◽  
Lectin Binding ◽  
Surface Membrane ◽  
Flow Cytometric Analysis ◽  
Peripheral Blood Lymphocytes ◽  
Blood Lymphocytes ◽  
Human Peripheral Blood Lymphocytes ◽  
Lentil Lectin

The binding of fluorescein-conjugated lentil lectin and concanavalin A to the surface membrane of human peripheral blood lymphocytes was studied by flow cytometry. The lymphocytes bound 3-fold more lentil lectin molecules compared with concanavalin A molecules and lentil lectin binding approached saturation at a much lower concentration than did that of concanavalin A. Lentil lectin identified two groups of lymphocytes: a low-binding T-cell fraction and a high-binding B-cell-enriched fraction. Concanavalin A did not discriminate between these populations in unseparated lymphocytes. Competition studies indicated that lentil lectin and concanavalin A were bound to different sites on the lymphocyte surface, although about 50% of lentil lectin sites were in close proximity to concanavalin A sites.

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