Isolation and characterization of cyanogen bromide fragments and a glycopeptide from the Dolichos biflorus lectin.

Biochemistry
W G Carter, M E Etzler

Abstract

The 110000 molecular weight Dolichos biflorus lectin is a glycoprotein composed of four subunits of approximately 27000 molecular weight with one methionine residue per subunit (Carter and Etzler, 1975b). Cyanogen bromide cleavage of the lectin yielded two fragments with approximate molecular weights of 15000 and 12000 as determined by electrophoresis on sodium dodecyl sulfate gels. Only the 15000 molecular weight fragment stained for carbohydrate with the periodic acid-Schiff stain. The two fragments were isolated, and their amino acid compositions were determined. The 15000 molecular weight fragment was identified as the amino terminal segment of the lectin subunits by NH2-terminal amino acid analysis. A glycopeptide with a minimum molecular weight of 1100 was isolated from the lectin by exhaustive Pronase digestion. Complete acid hydrolysis of the glycopeptide yielded aspartic acid, mannose, and N-acetylglucosamine in the ratio of 1:4-5:1-2. Partial acid hydrolysis of the glycopeptide produced a component which had an identical mobility with commercial N-acetylglucosaminylasparagine in high voltage paper electrophoresis. The data indicate that the carbohydrate unit of the lectin is bound to the amino terminal half of the sub...Continue Reading

References

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Citations

Jan 1, 1980·Neurochemistry International·C D Bridges, S L Fong
Nov 15, 1978·Biochimica Et Biophysica Acta·S L Biroc, M E Etzler
Dec 1, 1984·Plant Physiology·M E EtzlerS Thayer
Dec 1, 1989·Plant Physiology·J M Quinn, M E Etzler
Sep 1, 1987·European Journal of Biochemistry·D J SchnellM E Etzler
Oct 1, 1977·FEBS Letters·M E EtzlerP R Ziaya
Nov 1, 1987·Archives of Biochemistry and Biophysics·J M Quinn, M E Etzler
Sep 16, 1980·Biochemical and Biophysical Research Communications·M E Etzler, C Borrebaeck
Sep 1, 1975·FEBS Letters·R LotanN Sharon

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