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Lectin binding to the porcine and human ileal receptor of intrinsic factor-cobalamin.
Glycoconj J. 1989; 6(4):525-38.GJ

Abstract

The purified porcine receptor for the intrinsic factor-cobalamin complex bound to concanavalin A, lentil lectin and wheat germ lectin covalently coupled to Sepharose and was eluted with the corresponding soluble sugars. In contrast, human intrinsic factor bound efficiently to concanavalin A, to some extent to lentil lectin, but only slightly to wheat germ agglutinin. The binding of IF-Cbl to the receptor was inhibited when the receptor was pre-incubated with soluble wheat germ agglutinin, with an inhibition constant estimated to be 1.9 mumol/l. After transfer of the purified receptor from SDS-PAGE to Immobilon, ligand blotting of the purified receptor with iodinated lectin showed that concanavalin A and lentil lectin bound to three (75, 56 and 43 kDa) components but that wheat germ agglutinin bound only to the 75 kDa component. These results showed that the alpha subunit of the receptor could bind to wheat germ agglutinin, resulting in an inhibition of its binding with intrinsic factor. Both binding sites of intrinsic factor and of wheat germ agglutinin could be located near to each other.

Authors+Show Affiliations

Minerva Foundation Institute for Medical Research, Helsinki, Finland.No affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

2562509

Citation

Jokinen, O, et al. "Lectin Binding to the Porcine and Human Ileal Receptor of Intrinsic Factor-cobalamin." Glycoconjugate Journal, vol. 6, no. 4, 1989, pp. 525-38.
Jokinen O, Guéant JL, Schohn H, et al. Lectin binding to the porcine and human ileal receptor of intrinsic factor-cobalamin. Glycoconj J. 1989;6(4):525-38.
Jokinen, O., Guéant, J. L., Schohn, H., & Gräsbeck, R. (1989). Lectin binding to the porcine and human ileal receptor of intrinsic factor-cobalamin. Glycoconjugate Journal, 6(4), 525-38.
Jokinen O, et al. Lectin Binding to the Porcine and Human Ileal Receptor of Intrinsic Factor-cobalamin. Glycoconj J. 1989;6(4):525-38. PubMed PMID: 2562509.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Lectin binding to the porcine and human ileal receptor of intrinsic factor-cobalamin. AU - Jokinen,O, AU - Guéant,J L, AU - Schohn,H, AU - Gräsbeck,R, PY - 1989/1/1/pubmed PY - 1989/1/1/medline PY - 1989/1/1/entrez SP - 525 EP - 38 JF - Glycoconjugate journal JO - Glycoconj J VL - 6 IS - 4 N2 - The purified porcine receptor for the intrinsic factor-cobalamin complex bound to concanavalin A, lentil lectin and wheat germ lectin covalently coupled to Sepharose and was eluted with the corresponding soluble sugars. In contrast, human intrinsic factor bound efficiently to concanavalin A, to some extent to lentil lectin, but only slightly to wheat germ agglutinin. The binding of IF-Cbl to the receptor was inhibited when the receptor was pre-incubated with soluble wheat germ agglutinin, with an inhibition constant estimated to be 1.9 mumol/l. After transfer of the purified receptor from SDS-PAGE to Immobilon, ligand blotting of the purified receptor with iodinated lectin showed that concanavalin A and lentil lectin bound to three (75, 56 and 43 kDa) components but that wheat germ agglutinin bound only to the 75 kDa component. These results showed that the alpha subunit of the receptor could bind to wheat germ agglutinin, resulting in an inhibition of its binding with intrinsic factor. Both binding sites of intrinsic factor and of wheat germ agglutinin could be located near to each other. SN - 0282-0080 UR - https://www.unboundmedicine.com/medline/citation/2562509/Lectin_binding_to_the_porcine_and_human_ileal_receptor_of_intrinsic_factor_cobalamin_ L2 - http://RD3FS2PT9J.search.serialssolutions.com/openurl?url_ver=Z39.88-2004&res_dat=xri:pqm&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&genre=article&issn=0282-0080&eissn=1573-4986&volume=6&issue=4&spage=525&date=1989 DB - PRIME DP - Unbound Medicine ER -