Isolation and characterization of a new hemagglutinin from the red alga Gracilaria bursa-pastoris.
A new agglutinin has been isolated from the red alga Gracilaria bursa-pastoris by affinity chromatography on a yeast mannan-Cellulofine column. This agglutinin was isolated as a monomeric glycoprotein with a relatively low molecular weight. It had an isoelectric point of 4.7 and contained large amounts of Gly, Asx and Glx. It agglutinated trypsin-treated rabbit erythrocytes at the low concentration of 30 ng/ml. The activity was inhibited only by glycoproteins bearing N-glycans. This agglutinin also showed mitogenic activity for mouse splenic lymphocytes.
Okamoto
R
R
Faculty of Applied Biological Science, Hiroshima University, Japan.
Hori
K
K
Miyazawa
K
K
Ito
K
K
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002455:Cell Division / Q000187:drug effects; D002846:Chromatography, Affinity; D006384:Hemagglutination; D006388:Hemagglutinins / Q000302:isolation & purification* / Q000494:pharmacology; D007526:Isoelectric Point; D008214:Lymphocytes / Q000166:cytology / Q000187:drug effects; D051379:Mice; D008970:Molecular Weight; D011817:Rabbits; D000461:Rhodophyta / Q000032:analysis*
D000596:Amino Acids; D006388:Hemagglutinins