TY - JOUR
T1 - A novel lectin from sarcophaga
T2 - Its purification, characterization, and cDNA cloning
AU - Fujita, Yoshifumi
AU - Kurata, Shoichiro
AU - Homma, Ko Ichi
AU - Natori, Shunji
PY - 1998/4/17
Y1 - 1998/4/17
N2 - A novel C-type lectin that agglutinates rabbit red cells was purified from NIH-Sape-4 cells derived from the flesh fly (Sarcophaga peregrina), and its cDNA was isolated. This lectin, named granulocytin, appeared to be a trimer of a 20-kDa subunit consisting of 151 amino acid residues. The gene for granulocytin was activated in third instar larvae, and its expression was enhanced when the larval body wall was injured. In third instar larvae, granulocytin was found to be synthesized by hemocytes and secreted into the hemolymph. The molecular mass and gene expression patterns of granulocytin were very similar to those of Drosophila lectin that we reported previously (Haq, S., Kubo, T., Kurata, S., Kobayashi, A., and Natori, S. (1996) J. Biol. Chem. 271, 2021320218). However, these two lectins showed amine acid identifies of 20% at most, and no significant hapten sugar for granulocytin was identified.
AB - A novel C-type lectin that agglutinates rabbit red cells was purified from NIH-Sape-4 cells derived from the flesh fly (Sarcophaga peregrina), and its cDNA was isolated. This lectin, named granulocytin, appeared to be a trimer of a 20-kDa subunit consisting of 151 amino acid residues. The gene for granulocytin was activated in third instar larvae, and its expression was enhanced when the larval body wall was injured. In third instar larvae, granulocytin was found to be synthesized by hemocytes and secreted into the hemolymph. The molecular mass and gene expression patterns of granulocytin were very similar to those of Drosophila lectin that we reported previously (Haq, S., Kubo, T., Kurata, S., Kobayashi, A., and Natori, S. (1996) J. Biol. Chem. 271, 2021320218). However, these two lectins showed amine acid identifies of 20% at most, and no significant hapten sugar for granulocytin was identified.
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U2 - 10.1074/jbc.273.16.9667
DO - 10.1074/jbc.273.16.9667
M3 - Article
C2 - 9545300
AN - SCOPUS:0032540342
VL - 273
SP - 9667
EP - 9672
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 16
ER -