Purification and characterization of carbohydrate-binding peptides from Lotus tetragonolobusand Ulex europeus seed lectins using affinity chromatography

1992 ◽  
Vol 597 (1-2) ◽  
pp. 213-219 ◽  
Author(s):  
Yukiko Konami ◽  
Kazuo Yamamoto ◽  
Toshiaki Osawa
1979 ◽  
Vol 183 (2) ◽  
pp. 303-307 ◽  
Author(s):  
K Tryggvason ◽  
K Majamaa ◽  
J Risteli ◽  
K I Kivirikko

Prolyl 3-hydroxylase was purified up to about 5000-fold from an (NH4)2SO4 fraction of chick-embryo extract by a procedure consisting of affinity chromatography on denatured collagen linked to agarose, elution with ethylene glycol and gel filtration. The molecular weight of the purified enzyme is about 160000 by gel filtration The enzyme is probably a glycoprotein, since (a) its activity is inhibited by concanavalin A, and (b) the enzyme is bound to columns of this lectin coupled to agarose and can be eluted with a buffer containing methyl alpha-D-mannoside. The Km values for Fe2+, 2-oxoglutarate, O2 and ascorbate in the prolyl 3-hydroxylase reaction were found to be very similar to those previously reported for these co-substrates in the prolyl 4-hydroxylase and lysyl hydroxylase reactions.


1983 ◽  
Vol 6 (10) ◽  
pp. 737-747 ◽  
Author(s):  
YUKIKO KONAMI ◽  
KAZUO YAMAMOTO ◽  
TSUTOMU TSUJI ◽  
ISAMU MATSUMOTO ◽  
TOSHIAKI OSAWA

1983 ◽  
Vol 364 (1) ◽  
pp. 397-406 ◽  
Author(s):  
Yukiko KONAMI ◽  
Kazuo YAMAMOTO ◽  
Tsutomu TSUJI ◽  
Isamu MATSUMOTO ◽  
Toshiaki OSAWA

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