On the presence of two types of subunit in soybean agglutinin

Lotan, Reuben; Cacan, René; Cacan, Monique; Debray, Henri; Carter, William G.; Sharon, Nathan

doi:10.1016/0014-5793(75)80161-x

Cited by 44 publications

(14 citation statements)

References 12 publications

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“…Soybean lectin (SBA) which binds specifically to the N-acetyl-galactosamine (Ga1NAc) residue (16,17), stained two or three saccules in the cis region of the Golgi stack of the mucous cell at the bottom of the crypt (Fig. 1).…”

Section: Resultsmentioning

confidence: 99%

Ultracytochemistry of glycosylation sites of rat colonic mucous cells with labeled lectins.

Tsuyama

Suganuma

Ihida

et al. 1986

Acta Histochem. Cytochem

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Section: Resultsmentioning

confidence: 99%

Ultracytochemistry of glycosylation sites of rat colonic mucous cells with labeled lectins.

Tsuyama

Suganuma

Ihida

et al. 1986

Acta Histochem. Cytochem

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“…Soybean agglutinin which was initially reported to contain 4 identical subunits and two sugarbinding sites [6] was later shown by the same laboratory to contain dissimilar subunits [7] and 4 binding sites [S]. Goldstein and his co-workers could measure only two N-acetyl-D-galactosamine binding sites on the homotetrameric lectin (component III) from lima bean [9].…”

Section: Discussionmentioning

confidence: 99%

Four identical subunits in jack fruit seed agglutinin offer only two saccharide binding sites

Appukuttan

1985

FEBS Letters

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Gel filtration of jack fruit seed agglutinin in 6 M guanidine hydrochloride confirmed our earlier report that the native 39.5kDa protein was a tetramer of identical noncovalently associated IO-kDa subunits. Binding studies by the fluorescence quenching method using 4-methylumbelliferyl a-D-galactoside as well as equilibrium dialysis using p-nitrophenyl cr-D-galactoside indicated only two binding sites per tetramer. This behaviour resembles the half-of-the-sites reactivity in certain enzymes and is discussed in view of the small subunit size.Jack fruit seed agglutinin Half-of-the-sites binding Equilibrium dialysis Fluorescence quenching

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“…slightly different electrophoretic mobilities as determined by discontinuous polyacrylamide gels containing SDS (19). The Kunitz trypsin inhibitor of soybean is one of the best characterized of all plant proteinase inhibitors.…”

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Isolation and Characterization of Messenger RNAs for Seed Lectin and Kunitz Trypsin Inhibitor in Soybeans

Vodkin¹

1981

Plant Physiol.

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The mRNAs for seed lectin and Kuntz tpin inbitor of In addition to substantial biochemical data for these two seed proteins, lectin and trypsin inhibitor have been defined by classical genetic analyses and soybean varieties which lack detectable SBL or SBTI protein have been found (21,22,24). It is the aim of this report and other studies in progress to determine what molecular defects cause the inherited absence of SBL or SBTI protein in certain soybean varieties. Such knowledge will help elucidate the normal functioning and expression of plant genes. As an initial step toward this objective, I have developed modifications to a polysome immunoadsorption procedure which have allowed the isolation of highly enriched mRNAs for lectin and Kunitz trypsin inhibitor. A preliminary report has been published (33). The selected mRNAs were analyzed by their activities in a rabbit reticulocyte cell free translation system and by hybridization of labeled SBL or SBTI cDNA to gel blots of total poly(A) RNA.

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On the presence of two types of subunit in soybean agglutinin

Cited by 44 publications

References 12 publications

Ultracytochemistry of glycosylation sites of rat colonic mucous cells with labeled lectins.

Ultracytochemistry of glycosylation sites of rat colonic mucous cells with labeled lectins.

Four identical subunits in jack fruit seed agglutinin offer only two saccharide binding sites

Isolation and Characterization of Messenger RNAs for Seed Lectin and Kunitz Trypsin Inhibitor in Soybeans

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