Isolation and characterization of concanavalin A polypeptide chains

Biochemistry ◽  
1971 ◽  
Vol 10 (19) ◽  
pp. 3554-3559 ◽  
Author(s):  
Allen B. Edmundson ◽  
Kathryn R. Ely ◽  
Dayle A. Sly ◽  
Florence A. Westholm ◽  
Dennis A. Powers ◽  
...  
1981 ◽  
Vol 11 (11) ◽  
pp. 937-942 ◽  
Author(s):  
Jozef van Damme ◽  
Marc De Ley ◽  
Hendrik Claeys ◽  
Alfons Billiau ◽  
Carl Vermylen ◽  
...  

1978 ◽  
Vol 42 (4) ◽  
pp. 851-859
Author(s):  
Gunki Funatsu ◽  
Takashi Mise ◽  
Hideki Matsuda ◽  
Masaru Funatsu

Purified fractions of nuclei from rat liver and isolated calf thymocytes are treated with 0.5 M MgCl 2 or with an alkaline buffer, pH 8.5. Such procedures dissociate nuclear membranes from the chromatin. The membranes are simply floated in a gradient. The recovery in the membrane band obtained by the Mg 2+ technique is 55 to 60 %. Freeze-etching studies of the membrane pellets provide a good way to check their purity, pores being very conspicuous. A 5'-nucleotidase and an ATPase are detected on the nuclear membranes of thymocytes, as well as a still undescribed 3'-nucleotidase. However, no marker enzymes for the nuclear membrane have been found. The topology of sugar residues on the nuclear membranes is studied by means of lectins. Concanavalin A binds in large amounts to nuclear envelopes, both on the inner and outer leaflets, but not to pores.


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