Isolation and characterization of a sialic acid-specific binding lectin from the hemolymph of Asian horseshoe crab, tachypleus tridentatus

1993 ◽  
Vol 1156 (3) ◽  
pp. 255-262 ◽  
Author(s):  
Isami Tsuboi ◽  
Masahito Matsukawa ◽  
Nobuyuki Sato ◽  
Shoji Kimura
1981 ◽  
Vol 209 (1) ◽  
pp. 325-333 ◽  
Author(s):  
D.Thambi Dorai ◽  
B.K. Bachhawat ◽  
S. Bishayee ◽  
K. Kannan ◽  
D.Rajagopal Rao

2009 ◽  
Vol 10 (6) ◽  
pp. 1879-1881 ◽  
Author(s):  
Qiong-Zhen Li ◽  
Qi Li ◽  
Jun Liu ◽  
Le-Hai Ni ◽  
Ling-Feng Kong

1973 ◽  
Vol 135 (4) ◽  
pp. 875-880 ◽  
Author(s):  
James H. Nichols ◽  
Anatoly Bezkorovainy

A glycoprotein was isolated from the M-1 acid glycoprotein fraction of human colostrum. It had a molecular weight of 31200 and contained 27% galactose, 21.7% hexosamine, 8.0% fucose and 10.8% sialic acid by weight. The glycoprotein had no absorption maxima in the 240–300nm region, and was virtually free of ABH(O) and M and N blood-group activity. Alkaline borohydride cleavage of the glycoprotein resulted predominantly in the destruction of threonine and galactosamine.


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