The surface structure of erythrocytes from some animal sources

Seaman, G. V. F.; Uhlenbruck, G.

doi:10.1016/0003-9861(63)90117-6

Cited by 201 publications

(71 citation statements)

References 24 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…The sialic acid of erythrocytes has been studied extensively (9,20,21), and the amount of this substance that should be released under given conditions can be predicted with reasonable confidence. In every study, the amount of sialic acid released after neuraminidase treatment of intact erythrocytes for 2 hours or acid hydrolysis of equivalent amounts of During an identical period of incubation with influenza PR8 virus, only 6.5 ug sialic acid was released by the action of viral enzyme, or approximately two-thirds as much as by bacterial neuraminidase.…”

Section: Methodsmentioning

confidence: 99%

Sialic Acid of Human Blood Platelets*

Madoff¹,

Ebbe²,

Baldini³

1964

J. Clin. Invest.

View full text Add to dashboard Cite

Sialic acid has been demonstrated in the blood platelets of man and other species (1, 2), but its function in these elements is unknown. Jerushalmy, Kohn, and de Vries (3) and others (4,5) have shown that Myxoviruses are adsorbed to and eluted from blood platelets. Bacterial neuraminidase, which liberates free sialic acid by cleavage of the a-ketosidic linkage between terminal sialic acid and galactose or galactosamine (6), interferes with these platelet adsorptionelution phenomena (3) in a manner qualitatively similar to its effect on erythrocytes (7) and leukocytes (8). The electrophoretic mobility of platelets is reduced after neuraminidase treatment (3), again mimicking the behavior of the other blood elements (9, 10).Our investigations have yielded previously unknown data concerning the type and distribution of sialic acid in the platelet and its availability to viral and bacterial neuraminidases. Materials and MethodsHuman group 0, Rh-positive blood was collected by antecubital puncture into plastic bags containing EDTA anticoagulant 1 (1.5% disodium ethylenediaminetetraacetate in 0.7%o NaCl). The plasma was separated by centrifugation at 290 X g at 40 C for 25 minutes in an In-

show abstract

Section: Methodsmentioning

confidence: 99%

Sialic Acid of Human Blood Platelets*

Madoff¹,

Ebbe²,

Baldini³

1964

J. Clin. Invest.

View full text Add to dashboard Cite

show abstract

“…Thus an amino acid carboxyl group is substituted on the surface for the sialic acid carboxyl group, the net result being a similar or slightly elevated electrophoretic mobility ; a similar explanation has been used by Seaman and Uhlenbruck (1963) to explain analogous behavior of certain erythrocytes.…”

Section: Electrophoretic Mobilities Of Isolated Rat Liver Nuclei or Nmentioning

confidence: 79%

Molecules at the External Nuclear Surface

Bosmann

1973

The Journal of Cell Biology

View full text Add to dashboard Cite

The molecules occurring as terminal residues on the external surfaces of nuclei prepared from rat liver by either sucrose-CaC12 or citric acid methods and nucleoli derived from the sucrose-CaC1 2 nuclei were studied chemically and electrokinetically . In 0.0145 M NaCl, 4 .5 0 /,) sorbitol, and 0 .6 mM NaHCO3 with pH 7 .2 t 0 .1 at 25°C, the sucrose-CaC12 nuclei had an electrophoretic mobility of -1 .92 ,um/s/V/cm, the citric acid nuclei, -1 .63 µm/s/V/cm, and the nucleoli, -2 .53 µm/s/V/cm . The citric acid nuclei and the nucleoli contained no measurable sialic acid . The sucrose-CaC12 nuclei contained 0.7 pmol of sialic acid/mg nuclear protein ; this was essentially located in the nuclear envelope . Treatment of these nuclei with 50 µg neuraminidase/mg protein resulted in release of 0 .63 pmol of sialic acid/mg nuclear protein ; treatment with 1 % trypsin caused release of 0 .39 nmol of the sialic acid/mg nuclear protein . The pH-mobility curves for the particles indicated the sucrose-CaC12 nuclei surface had an acid-dissociable group of pK -2 .7 while the pK for the nucleoli was considerably lower . Nucleoli treated with 50 µg neuraminidase/mg particle protein had a mobility of -2 .53 Am/s/V/cm while sucrose-CaC12 nuclei similarly treated had a mobility of -1 .41 µm/s/V/cm . Hyaluronidase at 50 µg/mg protein had no effect on nucleoli mobility but decreased the sucrose-CaC12 nuclei mobility to -1 .79 M.m/s/V/cm . Trypsin at 1 % elevated the electrophoretic mobility of the sucrose-CaC12 nuclei slightly but decreased the mobility of the nucleoli to -2 .09 µm/s/V/cm . DNase at 50 Ag/mg protein had no effect on the mobility of the isolated sucrose-CaC12 nuclei but decreased the electrophoretic mobility of the nucleoli to -1 .21 µm/s/V/cm . RNase at 50 µg/mg protein also had no effect on the electrophoretic mobility of the sucrose-CaC12 nuclei but decreased the nucleoli mobility to -2 .10 µm/s/V/cm . Concanavalin A at 50 Ag/mg protein did not alter the nucleoli electrophoretic mobility but decreased the sucrose-CaC1 2 nuclei electrophoretic mobility to -1 .64 µm/s/V/cm . The results are interpreted to mean that the sucrose-CaC1 2 nuclear external surface contains terminal sialic acid residues in trypsin-sensitive glycoproteins, contains small amounts of hyaluronic acid, is completely devoid of nucleic acids, and binds concanavalin A . The nucleolus surface is interpreted to contain a complex made up of protein, RNA, and primarily DNA, to be devoid of sialic acid and hyaluronic acid, and not to bind concanavalin A.

show abstract

“…Previous studies indicate that the candidates most likely for anionic sites in the cell membrane are sulfate groups, found in acid mucopolysaccharides, ionized phosphate groups, found in phospholipids, and charged carboxyl groups largely due to the presence of sialic acid and from carboxyl groups from acidic amino acids of proteins (Ambrose 1966, Burry and Wood 1979, Eylar et al 1962, Seaman and Uhlenbruck 1963, Gasic et al 1968.…”

Section: Surface Chargementioning

confidence: 99%

The surface charge of trypanosomatids

Souto-Padrón

2002

An. Acad. Bras. Ciênc.

View full text Add to dashboard Cite

The surface charge of trypanosomatids was evaluated by means of the binding of cationic particles, as visualized by electron microscopy and by direct measurements of the electrophoretic mobility of cells. The results obtained indicate that most of the trypanosomatids exhibit a negatively charged surface whose value is species specific and varies according to the developmental stages. Sialic acids associated with glycoproteins, glycolipids and phosphate groups are the major components responsible for the net negative surface charge of the trypanosomatids.

show abstract

The surface structure of erythrocytes from some animal sources

Cited by 201 publications

References 24 publications

Sialic Acid of Human Blood Platelets*

Sialic Acid of Human Blood Platelets*

Molecules at the External Nuclear Surface

The surface charge of trypanosomatids

Contact Info

Product

Resources

About