Purification and Properties of Blood‐Group‐Specific Lectins from <i>Vicia cracca</i>

Rüdiger, Harold

doi:10.1111/j.1432-1033.1977.tb11255.x

Cited by 51 publications

(17 citation statements)

References 23 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Like This property (pH-sensitivity) has been observed in several other cases, however, even in a legume lectin of very different structure (12).…”

Section: Abstiracimentioning

confidence: 98%

“…Like This property (pH-sensitivity) has been observed in several other cases, however, even in a legume lectin of very different structure (12).In previous studies, we noted that crude extracts of Sophora leaves contained hemagglutinin activity and also displayed strong immunological cross-reactions with antisera raised against the Sophora seed lectin. In this report, we describe the purification and some of the properties of two lectins from Sophora leaves.…”

mentioning

confidence: 93%

See 1 more Smart Citation

The Lectins of Sophora japonica

Hankins

Kindinger²,

Shannon³

1987

Plant Physiol.

View full text Add to dashboard Cite

ABSTIRACITwo lectins, Leaf Lectin I and Leaf Lectin II (LLI and LLII) were purified from the leaves of Sophora japonica. Like This property (pH-sensitivity) has been observed in several other cases, however, even in a legume lectin of very different structure (12).In previous studies, we noted that crude extracts of Sophora leaves contained hemagglutinin activity and also displayed strong immunological cross-reactions with antisera raised against the Sophora seed lectin. In this report, we describe the purification and some of the properties of two lectins from Sophora leaves. MATERIALS AND METHODSThe tissues used in these studies were harvested from a single specimen of Sophora japonica, growing on the campus of the University of California, Riverside. Seeds were harvested when fully desiccated and stored at room temperature after removal from their pods. Fully expanded, mature leaves were harvested, washed with distilled H20, and if not extracted immediately, were frozen with liquid N2 and stored at -20C for later use.Extraction. All procedures were carried out at 0 to 5C unless otherwise specified. Leaves (200 g) were blended 2 min in a 4 L Waring Blendor with 1 L of distilled H20 containing 10 mM 3-mercaptoethanol and then squeezed through four layers of cheesecloth. The extract was then centrifuged (l0,OOOg) for 20 min to yield a clarified crude extract. The pH ofthe crude extract was lowered to 4.0 by the dropwise addition ofglacial acetic acid while stirring and after 30 min the resulting precipitate removed by centiifugation and discarded as before, yielded the pH supernatant. An equal volume of ice-cold acetone was added dropwise to the pH supernatant over a period of 30 min while stirring on ice, then allowed to stand on ice for 30 min. The material precipitated by acetone was collected by centrifugation (50OOg x 10 min) and suspended in 100 ml of distilled H20. A substantial amount of insoluble material was removed by centrifugation (5000g, 10 min) and discarded.

show abstract

“…Like This property (pH-sensitivity) has been observed in several other cases, however, even in a legume lectin of very different structure (12).…”

Section: Abstiracimentioning

confidence: 98%

mentioning

confidence: 93%

The Lectins of Sophora japonica

Hankins

Kindinger²,

Shannon³

1987

Plant Physiol.

View full text Add to dashboard Cite

show abstract

“…(ethyleneglyco1) 20000. The GalNAc-specific lectin was removed from the extract according to the procedure described earlier [8]. Then the mannose/glucose-binding lectin was adsorbed to a column of Sephadex G-100.…”

Section: Sequence Analysiamentioning

confidence: 99%

Purification and Characterization of a Mannose/Glucose‐Specific Lectin from Vicia cracca

Baumann

Strosberg

Rüdiger

1982

European Journal of Biochemistry

Self Cite

View full text Add to dashboard Cite

The seeds of Vicia cracca are known to contain two lectins: an N‐acetylgalactosamine‐binding lectin, which reacts specifically with human erythrocytes of blood group A, and a mannose/glucose‐binding lectin unspecific towards human blood groups. The second lectin is the object of the present work. Purification was achieved by affinity chromatography on Sephadex G‐100. The native lectin has a molecular weight of 44000. It is composed of two small (Mr 5700) and two large subunits (Mr 17500). Binding of sugars to the lectin was assayed by equilibrium dialysis and spectrophotometrically; the association constants for glucose are 1.38×103 l/mol and 2.5×102 l/mol respectively. The primary structure of the small subunit was determined by analyses of the whole chain, of tryptic and CNBr peptides. It was shown to consist of 53 amino acid residues. The mannose/glucose‐binding lectin from Vicia cracca is highly homologous to the lectins from Vicia sativa, Vicia faba, Pisum sativum and Lens culinaris. There is, however, only limited homology to the N‐acetylgalactosamine‐specific lectin from Vicia cracca.

show abstract

“…These results are comparable to the human blood group A specificity exhibited by N-acetyl-D-glucosamine-specific lectins from seeds of Dolichos biflorus 21) and Vicia cracca. 22) Compared with the specificity for rabbit RBC, QIL was found to be 16 times less specific for human blood group A or B and 8 times less specific for human blood group AB. These results are similar to those for rice (Oryza sativa) lectin, which has no human blood group specificity but agglutinates rabbit erythrocytes more efficiently than erythrocytes from other animal species.…”

Section: Discussionmentioning

confidence: 99%