In:
Proceedings of the National Academy of Sciences, Proceedings of the National Academy of Sciences, Vol. 63, No. 4 ( 1969-08), p. 1439-1446
Abstract:
Trypsin treatment of human erythrocytes releases a soluble glycopeptide which binds to phytohemagglutinin and abolishes the erythroagglutinating and lymphocyte-stimulating properties of this molecule. The glycopeptide has been purified by alkaline borohydride treatment, proteolytic digestion, gel filtration, and DEAE-cellulose chromatography. The most highly purified glycopeptide has a molecular weight of about 2,000. The specificity for binding to phytohemagglutinin resides in the oligosaccharide portion of the molecule with the determinant sugar being a galactose residue which is penultimate to a N -acetylneuraminic acid in some chains and uncovered in others. The glycopeptide is about 3,000 times more potent than either N -acetylgalactosamine or galactose in inhibiting the mitogenic response of lymphocytes induced by phytohemagglutinin.
Type of Medium:
Online Resource
ISSN:
0027-8424
,
1091-6490
DOI:
10.1073/pnas.63.4.1439
Language:
English
Publisher:
Proceedings of the National Academy of Sciences
Publication Date:
1969
detail.hit.zdb_id:
209104-5
detail.hit.zdb_id:
1461794-8
SSG:
11
SSG:
12
