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Literature DB >> 7458903

Subunit structure of Vicia graminea anti-(blood-group N) lectin.

Abstract

The subunit of the Vicia graminea lectin with blood-group-N specificity was examined by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis and gel filtration in 6M-guanidinium chloride, and its molecular weights was found to be 25 000. The unique N-terminal sequence fof the first nine residues of the lectin confirmed that Vicia lectin consists of four identical chains non-covalently linked. Finally the microheterogeneity of the lectin shown by analytical isoelectric focusing is discussed.

Entities: Chemical

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Year: 1980 PMID： 7458903 PMCID： PMC1161931 DOI： 10.1042/bj1890185

Source DB: PubMed Journal: Biochem J ISSN： 0264-6021 Impact factor: 3.857

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References

21 in total

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Authors: J Margolis; K G Kenrick
Journal: Biochem Biophys Res Commun Date: 1967-04-07 Impact factor: 3.575

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Authors: Y Abe; M Iwabuchi; S I Ishii
Journal: Biochem Biophys Res Commun Date: 1971-12-03 Impact factor: 3.575

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Authors: B B Agrawal; I J Goldstein
Journal: Arch Biochem Biophys Date: 1968-03-20 Impact factor: 4.013

Subunit structure of Vicia graminea anti-(blood-group N) lectin.

1. Electrophoresis in polyacrylamide concentration gradient.

2. Multiple forms in the subunit structure of concanavalin A.

3. Protein-carbohydrate interaction. VII. Physical and chemical studies on concanavalin A, the hemagglutinin of the jack bean.

4. Isoelectric heterogeneity of bovine plasma albumin.

5. The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis.

6. The estimation of polypeptide chain molecular weights by gel filtration in 6 M guanidine hydrochloride.

7. Anti-estradiol antibodies: isoelectric focusing in polyacrylamide gel.

8. Estimation of molecular radius, free mobility, and valence using polyacylamide gel electrophoresis.

9. A protein sequenator.

10. Multiple hemagglutinins in soybean.