Plant Physiology 83:825-829 (1987)
© 1987 American Society of Plant Biologists
Development and Growth Regulation
The Lectins of Sophora japonica
I. Purification Properties and N-Terminal Amino Acid Sequences of Two Lectins from Leaves
Charles N. Hankins,
Juanita Kindinger and
Leland M. Shannon
Department of Biochemistry, University of California, Riverside, California 92521
Two lectins, Leaf Lectin I and Leaf Lectin II (LLI and LLII) were purified from the leaves of Sophora japonica. Like the Sophora seed lectin, LLI and LLII are tetrameric glycoproteins containing a single subunit with respect to size. The subunits of LLI (32 kilodaltons) and LLII (34 kilodaltons) are slightly larger than those of the seed lectin (29.5 kilodaltons). The three Sophora lectins display indistinguishable specificities, amino acid compositions, specific hemagglutinin activities, and extinction coefficients. Although very closely related to the seed lectin, the leaf and seed lectins are not immunologically identical and they differ in subunit molecular weights, carbohydrate content, and in the pH sensitivity of their hemagglutinin activities. N-terminal amino acid sequence analysis shows that although they are homologous proteins, the three Sophora lectins are products of distinct genes.
This article has been cited by other articles:
|
|
|
|
 
W. Wang, B. Hause, W. J. Peumans, G. Smagghe, A. Mackie, R. Fraser, and E. J.M. Van Damme
The Tn Antigen-Specific Lectin from Ground Ivy Is an Insecticidal Protein with an Unusual Physiology
Plant Physiology,
July 1, 2003;
132(3):
1322 - 1334.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
E. M. Herman and B. A. Larkins
Protein Storage Bodies and Vacuoles
PLANT CELL,
April 1, 1999;
11(4):
601 - 614.
[Full Text]
|
|
|
|
|
