Chitin-binding proteins from cowpea (Vigna unguiculata) seeds.
Vicilins (7S storage proteins) from cowpea (Vigna unguiculata) and other legume seeds were shown to bind to chitin, to regenerated chitin (fully acetylated chitin) and to chitosan (deacetylated chitin). Adsorbed vicilins were desorbed from these matrices by acetic and hydrochloric acids and by highly polymerized soluble chitosan. Proteins such as the lectin of common bean (PHA), soybean trypsin inhibitor (Kunitz), a beta-1,3-glucanase from cowpea seeds, bovine pancreatic alpha-chymotrypsin, chicken ovalbumin, serum albumin and rabbit gamma-globulin did not bind. The present result is the first description of vicilin binding to chitin but other proteins, such as wheat germ agglutinin (WGA), a lectin that contains the so called "chitin-binding domain", and a chitinase isolated from cowpea seeds, which are involved in the defense mechanisms of plants against insects and fungi, were also shown to bind to chitin as previously reported. The binding of vicilins to chitin is probably effected not through a "chitin-binding domain" because they do not share this sequence with the defense-related proteins cited above. We propose that this association of vicilins with chitin may be related to the effect of variant vicilins on the development of Callosobruchus maculatus (bruchid) in resistant cowpea seeds.
Sales
M P
MP
Departamento de Bioquímica e Biologia Molecular, Universidade Federal do Ceará, Fortaleza, CE, Brasil.
Gomes
V M
VM
Fernandes
K V
KV
Xavier-Filho
J
J
D005591:Chemical Fractionation; D002686:Chitin / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D010940:Plant Proteins / Q000737:chemistry / Q000378:metabolism*; D055314:Seed Storage Proteins; D012639:Seeds / Q000378:metabolism*
D010940:Plant Proteins; D055314:Seed Storage Proteins; D002686:Chitin; C015575:vicilin protein, plant