Document Detail

The purification, composition, and specificity of the anti-T lectin from peanut (Arachis hypogaea).
MedLine Citation:
PMID:  811657     Owner:  NLM     Status:  MEDLINE    
Peanut agglutinin was purified by affinity chromatography on Sepharose-epsilon-aminocaproyl-beta-D-galactopyranosylamine. The purified lectin obtained in a yield of 150 mg/100 g of defatted peanut was homogeneous on polyacrylamide gel electrophoresis, ultracentrifugation, and gel filtration. This intrinsic sedimentation coefficient (So20,w) and the intrinsic diffusion coefficient (Do20,w) were estimated at pH 7.4 as 5.7 +/- 0.1 S and 5.0 X 10(-7) cm2s(-1), respectively. The molecular weight of the agglutinin, determined by sedimentation and diffusion and by gel filtration, was found to be 110,000. Disc gel electrophoresis and gel filtration, both in the presence of sodium dodecyl sulfate, gave a single component of Mr = 27,500 suggesting that the lectin is a tetramer composed of four subunits. Four alanine residues per 110,000 g were found by NH2-terminal analysis and the sequence of the five NH2-terminal amino acids was: ALa-Glu-Ser-Val-Thr. Each cycle in a sequenator gave a single amino acid, suggesting that the four subunits are identical. Peanut agglutinin does not contain covalently bound sugar; it is devoid of cysteine and cystine, low in methionine, histidine, and tryptophan, but rich in acidic and hydroxyamino acids. The lectin agglutinated erthrocytes of human ABO blood types equally well, but only after they have been treated with neuraminidase. Of the monosaccharides tested for inhibition of hemagglutination only D-galactose and alpha- and beta-D-galactosides were active. High inhibitory activity was found with the Discaccharide DGalbeta(1 in equilibrium 3)DGalNAc and with the disialylated glycoproteins: alpha1-acid glycoprotein, fetuin, glycophorin, and human blood group NN or MM antigen. These desialylated glycoproteins also reacted with the lectin to form precipitin bands in Ouchterlony double diffusion in agar.
R Lotan; E Skutelsky; D Danon; N Sharon
Related Documents :
1473607 - Bovine proacrosin from cauda epididymal sperm: purification, characterization and parti...
17824717 - Cooperativity and selectivity in chemomechanical polyethylenimine gels.
647477 - Biosynthesis of chloramphenicol in streptomyces sp. 3022a. properties of an aminotransf...
15740067 - 11s and 7s globulins of coconut (cocos nucifera l.): purification and characterization.
339867 - Cellular content of the krebs cycle keto acids in yeasts grown on different nitrogen so...
8611947 - Determination of lactic acid and pyruvic acid in serum and cerebrospinal fluid by ion-e...
Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  250     ISSN:  0021-9258     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  1975 Nov 
Date Detail:
Created Date:  1976-02-09     Completed Date:  1976-02-09     Revised Date:  2009-10-27    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  8518-23     Citation Subset:  IM    
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Amino Acid Sequence
Amino Acids / analysis
Arachis hypogaea
Binding Sites
Chromatography, Affinity
Hemagglutination Tests
Lectins / analysis*,  immunology,  isolation & purification
Macromolecular Substances
Molecular Weight
Plant Lectins
Protein Binding
Protein Conformation
Reg. No./Substance:
0/Amino Acids; 0/Lectins; 0/Macromolecular Substances; 0/Plant Lectins

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

Previous Document:  Co-oxygenation of organic substrates by the prostaglandin synthetase of sheep vesicular gland.
Next Document:  Studies on thyroid hormone-binding proteins. II. Binding of thyroid hormones, retinol-binding protei...