Studies on a phytohemagglutinin from the lentil

Stein, Marshall D.; Howard, Irmgard K.; Sage, Harvey J.

doi:10.1016/s0003-9861(71)80074-7

Cited by 78 publications

(14 citation statements)

References 11 publications

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“…By equilibrium dialysis and by gel filtration on columns of Sephadex in equilibrium with the radioactive ligand, it was found that SBA contains two identical binding sites for N-acetyl-D-galactosamine per 120,000 daltons, with K= 3.0 × 104 l/mole (90). This value is close to that found for the association of methyl a-,-mannopyranoside to Con A (46,95) and of L-fucose the isolectins from Lotus tetragonolobus (96), but is considerably higher than the association constants for the binding of methyl a-D-glucoside and D-mannose to the lentil leetin (97).…”

Section: Chemical and Physical Properties Of Purified Lectinssupporting

confidence: 86%

The Biochemistry of Plant Lectins (Phytohemagglutinins)

Lis¹,

Sharon²

1973

Annu. Rev. Biochem.

974

236

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Section: Chemical and Physical Properties Of Purified Lectinssupporting

confidence: 86%

The Biochemistry of Plant Lectins (Phytohemagglutinins)

Lis¹,

Sharon²

1973

Annu. Rev. Biochem.

974

236

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“…Despite the fa ct that they are probably tetramers, the pea lectins have only two binding sites for mannose and methyl-a-D-glucoside (268), similar to what has been reported for the soybean (133) and lentil (254) lectins. Unlike Con A, the pea lectin retains its tetrameric structure after succinylation (267), although some reduction in mitogenic activity was noted as a result of this chemical modifica tion.…”

Section: Pea Lectinssupporting

confidence: 67%

“…Although the lentil lectin is generally regarded as being specific for simple a glycosides (101,254), a greater degree of inhibition is observed with complex glyco peptides isolated from human erythrocytes (35, 126, 13 1), transferrin (297), and IgM immunoglobulin (297). The substitution of the 0-2 position of mannose with N-acetylglucosamine causes a marked increase in inhibitory activity (1 15).…”

Section: Lentil Lectinsmentioning

confidence: 99%

Phytohemagglutinins (Phytolectins)

Liener¹

1976

Annu. Rev. Plant. Physiol.

234

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“…Nonquantitative adsorption was not due to a subpopulation of unglycosylated carboxylase since lentil lectin-Sepharose flow-through could be adsorbed to fresh lentil lectin (data not shown). Moreover, 100% of carboxylase activity could be adsorbed to concanavalin A-Sepharose, which has a much higher affinity than lentil lectin for mannosyl residues (27). Unfortunately, carboxylase activity could not be recovered at all from concanavalin A-Sepharose by using methyl a-mannoside and/or methyl a-glucoside (data not shown).…”

Section: Resultsmentioning

confidence: 99%

Purification and identification of bovine liver gamma-carboxylase.

Berkner¹,

Harbeck²,

Lingenfelter³

et al. 1992

Proc. Natl. Acad. Sci. U.S.A.

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The microsomal y-carboxylase catalyzes modification of a limited set of glutamyl residues to y-carboxyglutamyl residues in a vitamin K-dependent reaction that also utilizes 02 and CO2. We report the purification to apparent homogeneity of the bovine liver microsomal carboxylase. Affinity chromatography exploiting the association of the carboxylase with prothrombin precursor and carboxylase binding to the propeptide sequence were combined with ion-exchange chromatography and fractionation using immobilized lectins. A 3.5 x 105-fold purification was obtained, which is the highest purification, by a factor of 35, yet reported for this enzyme. A single 98-kDa protein is obtained from this isolation. Carboxylase activity is associated with this protein by two different criteria. Antibodies prepared against the carboxylase detected the 98-kDa protein when used in Western analysis. In addition, the single 98-kDa protein was shown to comigrate with activity when electrophoresed in a nondenaturing gel system. The availability of purified preparations of carboxylase will facilitate an increased understanding of the complex biochemical reaction carried out by this protein.The liver microsomal carboxylase catalyzes the posttranslational modification of selected glutamyl residues to Y-carboxylated glutamyl (Gla) residues in a limited set of proteins in a reaction requiring vitamin K hydroquinone, 02, and CO2 (1-3). These vitamin K-dependent proteins contain multiple glutamyl residues clustered at the N terminus in what is referred to as the Gla domain. Carboxylation of glutamyl residues in the Gla domain enables the Ca2+-mediated interaction ofthese proteins with phospholipids and is required for their biological activity. Vitamin K-dependent carboxylase activity has been detected in almost all mammalian tissues assayed and has been observed in one invertebrate as well (4). Its apparent presence in a wide variety of cultured lines can also be inferred from the ability of these lines to secrete carboxylated vitamin K-dependent recombinant proteins (5-10). A major limitation in understanding the mechanism of carboxylation has been the lack of a purified preparation of this enzyme. Attempts pmade using selective detergent extraction, ammonium sulfate fractionation, and conventional chromatography have been successful only in a limited purification (11-13). More recently, the propeptide sequence unique to all vitamin K-dependent proteins has been used in attempts to purify the carboxylase (14-16). This sequence is similar among vitamin K-dependent proteins that share very little other homology, leading to the proposal that the propeptide sequence is important for carboxylase recognition (17). The observations that mutations in protein C (18) or factor IX (19) impair carboxylation supported this concept. Carboxylase purifications have been attempted by using the propeptide as a ligand in affinity chromatography (15,16). The enzyme has also been isolated by virtue of its known association with its vitamin K-dependent prote...

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Studies on a phytohemagglutinin from the lentil

Cited by 78 publications

References 11 publications

The Biochemistry of Plant Lectins (Phytohemagglutinins)

The Biochemistry of Plant Lectins (Phytohemagglutinins)

Phytohemagglutinins (Phytolectins)

Purification and identification of bovine liver gamma-carboxylase.

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