Morniga M

About the Lectin

The bark of the black mulberry tree (Morus nigra)
accumulates large quantities of a galactose-specific (Morniga G) and a mannose (Man)-specific (Morniga M) jacalinrelated
lectin. Morniga G resembles jacalin with respect to its
molecular structure, specificity, and co-and posttranslational
processing indicating that it follows the secretory pathway
and eventually accumulates in the vacuolar compartment. In
contrast, Morniga M represents a novel type of highly active
Man-specific jacalin-related lectin that is synthesized without
signal peptide or other vacuolar targeting sequences, and
accordingly, accumulates in the cytoplasm. The isolation and
cloning, and immunocytochemical localization of Morniga G
and Morniga M not only demonstrates that jacalin-related
lectins act as vegetative storage proteins in bark, but also
allows a detailed comparison of a vacuolar galactose-specific
and a cytoplasmic Man-specific jacalin-related lectin from
a single species. Moreover, the identification of Morniga M
provides the first evidence, to our knowledge, that bark
cells accumulate large quantities of a cytoplasmic storage
protein. In addition, due to its high activity, abundance, and
ease of preparation, Morniga M is of great potential value
for practical applications as a tool and bioactive protein in
biological and biomedical research 1 .

REFERENCES

  1. Van Damme, Els, et al.(2002) Plant Physiology. 130 : 757-769

Product Characteristics

Buffer 0.01M Phosphate – 0.15M NaCl, pH 7.2-7.4.
Blood Group A.
Activity MNA-M has specific agglutination activity at 43 ng mL-1.
Inhibitory Carbohydrate MNA-M is specific for Mannose.
Molecular Weight MNA-G has a MW=16,000 and MNA-M has a doublet of MW=15,000 and 16,000 when analyzed by SDS-PAGE. Higher molecular weight species (>5 million Da) are present in samples analyzed by gel filtration.