1972
DOI: 10.1016/0014-4827(72)90181-4
|View full text |Cite
|
Sign up to set email alerts
|

Binding of positively charged particles to glutaraldehyde-fixed human erythrocytes

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2
1
1

Citation Types

2
13
0

Year Published

1972
1972
2016
2016

Publication Types

Select...
10

Relationship

2
8

Authors

Journals

citations
Cited by 52 publications
(15 citation statements)
references
References 10 publications
2
13
0
Order By: Relevance
“…2c). This effect is often ascribed to the higher affinity of positively charged species to negatively charged phospholipids in the cellular membrane (Weiss et al 1972). Arvizo et al found this effect to cause depolarization of plasma membrane potential.…”
Section: Membrane Penetration Uptake Efficiency Biodistribution Andmentioning
confidence: 99%
“…2c). This effect is often ascribed to the higher affinity of positively charged species to negatively charged phospholipids in the cellular membrane (Weiss et al 1972). Arvizo et al found this effect to cause depolarization of plasma membrane potential.…”
Section: Membrane Penetration Uptake Efficiency Biodistribution Andmentioning
confidence: 99%
“…2). However, 'as the distribution of negatively charged groups on mammalian cell surfaces does not appear to be homogeneous [12] one could envisage preferential contact of negatively charged liposomes with cell surface areas of lower than average surface charge [13]. It is also possible that the small size of liposomes could reduce the potential energy barrier opposing close contact with the cell surface [14,15].…”
Section: The Efiect Of the Surface Charge Of Liposomes On Their Elimimentioning
confidence: 99%
“…Differences have been 218 ThE JOURNAL OF CELL BIOLOGY 9 VOLUME 71, 1976 9 pages 218-231 found between various erythroid developmental stages in surface density of negative charges (34,36), cell surface antigenicity (22,38), and pyroantimonate (1) and Con A (2) binding. By using positively charged colloidal ferric oxide (which binds to sialic acid residues [12,20,42]) it was previously shown that the density of anionic groups in developing rabbit erythrocytes gradually decreases with successive divisions of the proerythroblasts, then reincreases after expulsion of the nucleus and on maturation of the reticulocyte to become a mature erythrocyte (13,15,36). If one assumes that the binding sites are associated with glycoproteins, these modulations in the surface charge density suggest that the rate of synthesis and insertion into the red blood cell membrane of different plasma membrane proteins varies at specific stages in the differentiation process.…”
mentioning
confidence: 99%