Abstract:

The primary storage protein of oat (Avena sativa L.) seeds, globulin, was shown to have a specific carbohydrate-binding activity. The globulin was capable of hemagglutinating rabbit red blood cells and this hemagglutination was inhibited by the beta-glucan, laminarin, as well as by carbohydrate which had been cleaved from the native globulin. Globulin with carbohydrate-binding activity was isolated from cell wall preparations and from defatted flour. The lectin activity apparently resides in the alpha-subunit of the globulin and has affinity for the carbohydrate which is O-glycosidically linked to the globulin. A portion of this carbohydrate is attached to the beta-subunit. Two affinity columns were synthesized utilizing laminarin and the carbohydrate from the native globulin as ligands. The hemagglutinating activity bound to both of these columns. The activity was specifically eluted from the globulin-carbohydrate affinity column with carbohydrate cleaved from native globulin by an alkali-catalyzed beta-elimination. The possible roles of this unique self-binding capacity are discussed.

Open in

PUBMED | PMC | Google Scholar | Wikipedia

Relations:

Content

Citations

(1)

References

(19)

Drugs

(2)

Affiliates

(1)

A Seed Storage Protein with Possible Self-Affinity through Lectin-Like Binding <sup><a href="#fn1" rid="fn1" class=" fn">1</a></sup>

P Langston-Unkefer

W Gade

Abstract

The primary storage protein of oat (Avena sativa L.) seeds, globulin, was shown to have a specific carbohydrate-binding activity. The globulin was capable of hemagglutinating rabbit red blood cells and this hemagglutination was inhibited by the β-glucan, laminarin, as well as by carbohydrate which had been cleaved from the native globulin. Globulin with carbohydrate-binding activity was isolated from cell wall preparations and from defatted flour. The lectin activity apparently resides in the α-subunit of the globulin and has affinity for the carbohydrate which is O-glycosidically linked to the globulin. A portion of this carbohydrate is attached to the β-subunit. Two affinity columns were synthesized utilizing laminarin and the carbohydrate from the native globulin as ligands. The hemagglutinating activity bound to both of these columns. The activity was specifically eluted from the globulin-carbohydrate affinity column with carbohydrate cleaved from native globulin by an alkali-catalyzed β-elimination. The possible roles of this unique self-binding capacity are discussed.

Full text

Full text is available as a scanned copy of the original print version. Get a printable copy (PDF file) of the complete article (2.1M), or click on a page image below to browse page by page. Links to PubMed are also available for Selected References.

Images in this article

Fig. 1
on p.677

Fig. 2
on p.678

Fig. 3
on p.678

Click on the image to see a larger version.

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

Barondes SH. Lectins: their multiple endogenous cellular functions. Annu Rev Biochem. 1981;50:207–231. [PubMed] [Google Scholar]
Baumann CM, Rüdiger H. Interactions between the two lectins from Vicia cracca. FEBS Lett. 1981 Dec 28;136(2):279–283. [PubMed] [Google Scholar]
Bohlool BB, Schmidt EL. Lectins: a possible basis for specificity in the Rhizobium--legume root nodule symbiosis. Science. 1974 Jul 19;185(4147):269–271. [PubMed] [Google Scholar]
Brinegar AC, Peterson DM. Separation and characterization of oat globulin polypeptides. Arch Biochem Biophys. 1982 Nov;219(1):71–79. [PubMed] [Google Scholar]
Brinegar AC, Peterson DM. Synthesis of Oat Globulin Precursors : Analogy to Legume 11S Storage Protein Synthesisa. Plant Physiol. 1982 Dec;70(6):1767–1769.[PMC free article] [PubMed] [Google Scholar]
Burr B, Burr FA, St John TP, Thomas M, Davis RW. Zein storage protein gene family of maize. An assessment of heterogeneity with cloned messenger RNA sequences. J Mol Biol. 1982 Jan 5;154(1):33–49. [PubMed] [Google Scholar]
Edge AS, Faltynek CR, Hof L, Reichert LE, Jr, Weber P. Deglycosylation of glycoproteins by trifluoromethanesulfonic acid. Anal Biochem. 1981 Nov 15;118(1):131–137. [PubMed] [Google Scholar]
Gade W, Jack MA, Dahl JB, Schmidt EL, Wold F. The isolation and characterization of a root lectin from soybean (Glycine max (L), cultivar Chippewa). J Biol Chem. 1981 Dec 25;256(24):12905–12910. [PubMed] [Google Scholar]
Gansera R, Schurz H, Rüdiger H. Lectin-associated proteins from the seeds of Leguminosae. Hoppe Seylers Z Physiol Chem. 1979 Nov;360(11):1579–1585. [PubMed] [Google Scholar]
Köhle H, Kauss H. Binding of Ricinus communis agglutinin to the mitochondrial inner membrane as an artifact during preparation. Biochem J. 1979 Dec 15;184(3):721–723.[PMC free article] [PubMed] [Google Scholar]
LOWRY OH, ROSEBROUGH NJ, FARR AL, RANDALL RJ. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
Mirelman D, Galun E, Sharon N, Lotan R. Inhibition of fungal growth by wheat germ agglutinin. Nature. 1975 Jul 31;256(5516):414–416. [PubMed] [Google Scholar]
Mishkind ML, Palevitz BA, Raikhel NV, Keegstra K. Localization of wheat germ agglutinin--like lectins in various species of the gramineae. Science. 1983 Jun 17;220(4603):1290–1292. [PubMed] [Google Scholar]
Paulovă M, Tichă M, Entlicher G, Kostĩr JV, Kocourek J. Studies on phytohemagglutinins. IX. Metal content and activity of the hemagglutinin from the lentil (Lens esculenta Moench). Biochim Biophys Acta. 1971 Nov 12;252(2):388–395. [PubMed] [Google Scholar]
Peterson DM. Subunit structure and composition of oat seed globulin. Plant Physiol. 1978 Oct;62(4):506–509.[PMC free article] [PubMed] [Google Scholar]
Plantner JJ, Carlson DM. Studies of mucin-type glycoproteins. Olefinic amino acids, products of the beta-elimination reaction. Anal Biochem. 1975 May 12;65(1-2):153–163. [PubMed] [Google Scholar]
Tumer NE, Thanh VH, Nielsen NC. Purification and characterization of mRNA from soybean seeds. Identification of glycinin and beta-conglycinin precursors. J Biol Chem. 1981 Aug 25;256(16):8756–8760. [PubMed] [Google Scholar]
Turner RH, Liener IE. The use of glutaraldehyde-treated erythrocytes for assaying the agglutinating activity of lectins. Anal Biochem. 1975 Oct;68(2):651–653. [PubMed] [Google Scholar]
Uy R, Wold F. 1,4-Butanediol diglycidyl ether coupling of carbohydrates to Sepharose: affinity adsorbents for lectins and glycosidases. Anal Biochem. 1977 Jul;81(1):98–107. [PubMed] [Google Scholar]

United States Department of Agriculture, Agricultural Research Service, University of Wisconsin, Madison, Wisconsin 53706

Department of Agronomy, University of Wisconsin, Madison, Wisconsin 53706

Department of Plant Pathology, University of Minnesota, St. Paul, Minnesota 55108

^{Cooperative investigation of the United States Department of Agriculture, Agricultural Research Service, and the College of Agricultural and Life Science, University of Wisconsin-Madison.}

Copyright notice

Abstract

The primary storage protein of oat (Avena sativa L.) seeds, globulin, was shown to have a specific carbohydrate-binding activity. The globulin was capable of hemagglutinating rabbit red blood cells and this hemagglutination was inhibited by the β-glucan, laminarin, as well as by carbohydrate which had been cleaved from the native globulin. Globulin with carbohydrate-binding activity was isolated from cell wall preparations and from defatted flour. The lectin activity apparently resides in the α-subunit of the globulin and has affinity for the carbohydrate which is O-glycosidically linked to the globulin. A portion of this carbohydrate is attached to the β-subunit. Two affinity columns were synthesized utilizing laminarin and the carbohydrate from the native globulin as ligands. The hemagglutinating activity bound to both of these columns. The activity was specifically eluted from the globulin-carbohydrate affinity column with carbohydrate cleaved from native globulin by an alkali-catalyzed β-elimination. The possible roles of this unique self-binding capacity are discussed.

Collaboration tool especially designed for Life Science professionals.Drag-and-drop any entity to your messages.

Learn More