Isolation of concanavalin a binding protein(s) from rat erythrocyte stroma

Akedo, Hitoshi; Mori, Yoichi; Tanigaki, Yumiko; Shinkai, Kiyoko; Morita, Kazuko

doi:10.1016/0005-2795(72)90213-9

Cited by 31 publications

(9 citation statements)

References 12 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The presence of multiple molecular species, which differ in their electrophoretie mobilities, has been observed upon electrophoresis of crystalline Con A at pH 2.4 and 7.4 (36) and upon electrofoeusing (37,68). Electrofocusing yielded as as eight differently migrating protein bands (68). Preincubation of Con with t)-mannose or D-glucose reduced the number of bands to two, with simultaneous shift in their isoelectric points (69).…”

Section: Chemical and Physical Properties Of Purified Lectinsmentioning

confidence: 94%

“…Development of turbidity pH 7 was eliminated by the addition of 0.01 M ~)-glucose. The presence of multiple molecular species, which differ in their electrophoretie mobilities, has been observed upon electrophoresis of crystalline Con A at pH 2.4 and 7.4 (36) and upon electrofoeusing (37,68). Electrofocusing yielded as as eight differently migrating protein bands (68).…”

Section: Chemical and Physical Properties Of Purified Lectinsmentioning

confidence: 96%

“…Recently, Con A from nata bean Canavalia gladiata has been purified and crystallized (68). This preparation resembled that from iack bean in its biological, chemical, and physical properties.…”

Section: Chemical and Physical Properties Of Purified Lectinsmentioning

confidence: 98%

“…In general, the procedures involve the release of membrane components by degradation with proteolytie enzymes (260)(261)(262)(263), hypotonie shock (264), or by solubilization with detergents (68,(265)(266)(267)(268). This is followed by purification of the receptors by gel filtration and ion exchange chromatography (260)(261)(262)(263)268), by isoelectrie focusing on polyacrylamide gels (68), or by affinity chromatography on Sepharose-bound lectins (266,267). The latter technique, only recently introduced, will certainly play an increasingly important role in the isolation of leetin receptor sites.…”

Section: Cell Receptors For Lectinsmentioning

confidence: 99%

See 3 more Smart Citations

The Biochemistry of Plant Lectins (Phytohemagglutinins)

Lis¹,

Sharon²

1973

Annu. Rev. Biochem.

974

236

View full text Add to dashboard Cite

Section: Chemical and Physical Properties Of Purified Lectinsmentioning

confidence: 94%

Section: Chemical and Physical Properties Of Purified Lectinsmentioning

confidence: 96%

Section: Chemical and Physical Properties Of Purified Lectinsmentioning

confidence: 98%

Section: Cell Receptors For Lectinsmentioning

confidence: 99%

See 2 more Smart Citations

The Biochemistry of Plant Lectins (Phytohemagglutinins)

Lis¹,

Sharon²

1973

Annu. Rev. Biochem.

974

236

View full text Add to dashboard Cite

“…The seeds of C. gladiata exhibit antiemetic and demulcent effects, and are used to stop hiccups in Chinese traditional medicine (Sridha and Seena, 2006). Gibberellins (Tamura et al, 1967), an amino acid (Schlucter and Bordas, 1972), and an enzyme (Akedo et al, 1972) have been reported as chemical constituents of Jack bean. The composition of the total FAs is often the only information provided from studies on bean lipids.…”

Section: Introductionmentioning

confidence: 99%

Characteristics of Lipid Components and Triacylglycerol Molecular Species of Jack Bean (Canavalia gladiata DC.)

Yoshida

Yoshida²,

Tomiyama-Sakamoto

et al. 2012

FSTR

View full text Add to dashboard Cite

An electron microscopic investigation of the surface coat of visceral yolk sac endoderm cells in the guinea pig

King

1974

Anat. Rec.

View full text Add to dashboard Cite

Guinea pig visceral yolk sac endoderm cells are known to absorb proteins from the uterine lumen by the process of pinocytosis. Since previous studies have shown that the first step in protein absorption is the binding of the protein to an extracellular material on the surface of pinocytotic invaginatiom, it was thought that the surface coat might possess receptor sites for molecules which are subsequently absorbed. This study investigates the nature of the surface coat of the endoderm cells using ruthenium red, alcian blue/cetylpyridynium chloride-lanthanum and concanavalin A-peroxidase procedures. Results using these methods showed the presence of a surface coat on both the microvilli and pinocytotic invaginations. The coat on the pinocytotic invaginations was thicker than that on the microvilli. Concanavalin A receptor sites were separated from one another on the cell surface. Since only those pinocytotic invaginations which were open to the surface at the time of fixation would be "stained" by these methods, the procedures also show that the numerous tubules and vesicles in the apical cytoplasm do not all form an intercommunicating labyrinth open to the surface, even though most of them are part of a related functional system. The results indicate that the surface coat contains mucopolysaccharide components. In addition, concanavalin A receptor sites are present which are probably oligosaccharides associated with a glycoprotein component of the apical cell membrane.

show abstract

Isolation of concanavalin a binding protein(s) from rat erythrocyte stroma

Cited by 31 publications

References 12 publications

The Biochemistry of Plant Lectins (Phytohemagglutinins)

The Biochemistry of Plant Lectins (Phytohemagglutinins)

Characteristics of Lipid Components and Triacylglycerol Molecular Species of Jack Bean (Canavalia gladiata DC.)

An electron microscopic investigation of the surface coat of visceral yolk sac endoderm cells in the guinea pig

Contact Info

Product

Resources

About