Purification and some properties of a lectin from the hemolymph of Periplaneta americana (American cockroach)
Open Access
- 1 October 1987
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 168 (1) , 75-82
- https://doi.org/10.1111/j.1432-1033.1987.tb13389.x
Abstract
A lectin showing specificity for human A-type red blood cells was purified to homogeneity from the hemolymph of the American cockroach Periplaneta americana by affinity chromatography on bovine submaxillary gland mucin. This lectin was a huge molecule with molecular mass of about 1500 kDa, with a single subunit of 30-kDa protein, and required Ca2+ for expression of lectin activity. Electron microscopic examination showed that these molecules were rods with helical structure with an average length of 50.5 nm and width of 10 nm. The molecule was suggested to contain tandemly aligned basic units of 10 nm length.This publication has 28 references indexed in Scilit:
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