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Lima-bean lectin

SPARVOLIF, GALLO A, MARiNELLi D, SANTUCCi A, BOLLiNi R (1998) Novel lectin-related proteins are major components in lima bean Phaseolus lunatus L.) seeds. Biochim Biophys Acta. 1382 311-23. [Pg.184]

Phaseolus lunatus lectins Phaseolus lunatus (lima bean) GalNAc... [Pg.501]

The lima-bean agglutinin holds the distinction of being the first lectin shown to exhibit blood-group specificity. Although Boyd initially observed, in 1945, that the lima-bean lectin specifically agglutinated type A erythrocytes,2,4 he did not publish his observation until 1949,... [Pg.243]

Lima-bean lectin precipitated blood-group A and B secretor saliva, but not O it did not precipitate the saliva of any nonsecretors.2,3,103 Kriipe77 substantiated Boyd s results, using secretor saliva as an inhibitor of lima-bean lectin-erythrocyte agglutination. Types A,B, A,A2, AiO, and A20 saliva all inhibited the lima-bean lectin, whereas type OO saliva and type OO ovarian-cyst material were noninhibitory. [Pg.244]

Boyd and coworkers583 also labelled lima-bean lectin with 131I (indirectly, by coupling of [131I]-p-iodoaniline to protein by diazotization)584 and visible dyes,584,585 and quantitated the binding to type A erythrocytes. [Pg.246]

Ions of Mn2+ and Ca2+ were bound to the purified, lima-bean lectins.151,199 Removal of Mn2+ lowered the hemagglutination titer by 75%. (Ethylenedinitrilo)tetraacetate completely inhibited the precipitin reaction between lima-bean lectin component III and type A blood-group substance (compare Ref. 579). Several divalent-metal cations restored activity to the demetallized protein or (ethylenedinitrilo)tetraacetate-treated lectin the addition of Ca2+,... [Pg.247]

The specific-titer activity of lima-bean lectin components II and III towards type A human erythrocytes was 5,100 and 1,300, respectively, and, towards type B erythrocytes, 20 and 5.1, respectively.151 199 The hemagglutinating activity of component II is, thus, four times the activity151,199 of component III. Neither component reacted with type O human, red blood-cells, or native or trypsinized, rabbit erythrocytes.151,199... [Pg.248]

The reaction of partially purified, lima-bean lectin with hog gastric-mucin type A substance exemplified the precipitin-like curve obtained for lectin-polysaccharide or -glycoprotein reactions.103 Classical precipitin-curves between purified components II and III and type A blood-group substance were also obtained.151,199 Maximal precipitation of component II (equivalence) occurred at a lower ratio of A substance per mole of protein than for component III. Under conditions where type A substance precipitated 90% of the lectin, types A2 and B precipitated151,199 66 and 13%, respectively, of component II, and 21 and 0% of component III. Neither of the lima-bean lectins precipitated with type O blood-group substance. [Pg.248]

Inhibition of the precipitation reaction between lima-bean lectin component III and human blood-group A substance.587,591... [Pg.249]

In view of its discovery as the first blood-group-specific lectin, it is surprising that the lima-bean lectin is still one of the least studied, plant agglutinins. Undoubtedly, this lectin merits closer scrutiny. [Pg.250]

Papain, Bandeiraea simplicifolia lectin, and lima bean lectin have been labeled with diazotized [ I]aniline according to the procedure described... [Pg.246]

The carbohydrate-binding specificity of the lima bean lectin studied by inhibition of precipitation, and a sulfhydryl group protection assay [161], revealed the type A trisaccharide GalNAc(al-3)[L-Fuc(al-2)]Gal to be the best inhibitor, 40 times more potent than GalNAc. The a-glycosides of GalNAc are 8 times more potent than the corresponding 3-anomers. [Pg.420]

Mirelman, D., Bracha, R. Sharon, N. (1974b) Penicillin-induced Secretion of a Soluble, Uncrosslinked Peptidoglycan by Micrococcus luteus Cells Biochemistry, 13, 5045-53 Misaki, A. Goldstein, I.J. (1977) Glycosyl Moiety of Lima Bean Lectin , Journal of Biological Chemistry, 252, 6995-9... [Pg.330]

Legumes are a rich source of lectins or phytohemagglutinins. Inadequately cooked legumes may cause lectin-induced disturbances and adverse nutritional effect in humans. Lima bean lectin contains exposed cysteinyl groups necessary for its activity. We assessed the ability of N-acetylcysteine to act synergistically with heat in destabilizing and inactivating this lectin in lima bean flour. [Pg.261]

Our study IS) revealed that the cysteine derivative facilitated inactivation of lima bean lectin in the temperature range 25 to 85°C and in the pH range 4.4 to 10.0. As with the protease inhibitors described above, the beneficial action of N-acetylcysteine is postulated to involve formation of mixed disulfide bonds between the cysteine derivative, lectins, and structural proteins in the flour. [Pg.261]

In contrast to the findings with lima bean lectins soybean lectins which contain no cysteinyl residues, were not affected by the thiol treatments. [Pg.261]


See other pages where Lima-bean lectin is mentioned: [Pg.269]    [Pg.2]    [Pg.5]    [Pg.233]    [Pg.128]    [Pg.130]    [Pg.138]    [Pg.145]    [Pg.164]    [Pg.244]    [Pg.244]    [Pg.245]    [Pg.245]    [Pg.246]    [Pg.246]    [Pg.247]    [Pg.247]    [Pg.248]    [Pg.249]    [Pg.250]    [Pg.324]    [Pg.324]    [Pg.404]    [Pg.408]    [Pg.419]    [Pg.419]    [Pg.420]    [Pg.684]    [Pg.16]    [Pg.1450]    [Pg.258]   
See also in sourсe #XX -- [ Pg.2 , Pg.5 ]




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