Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1938811 | Biochemical and Biophysical Research Communications | 2006 | 6 Pages |
Abstract
The N-terminal lectin domain (Nh) of the tandem repeat-type nematode galectin LEC-1 has a lower affinity for sugars than the C-terminal lectin domain. To confirm that LEC-1 forms a complex with N-acetyllactosamine-containing glycoproteins, we used several mutants of LEC-1 in which a unique cysteine residue was introduced into the Nh domain and examined their binding to bovine asialofetuin with a photoactivatable sulfhydryl crosslinking reagent. A crosslinked product was formed with the Q38C mutant, strongly suggesting the low-affinity interaction of Nh with the glycoprotein could be detected with this system.
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Authors
Yoichiro Arata, Mayumi Tamura, Takamasa Nonaka, Ken-ichi Kasai,