Immunological cross-reaction between bud and bark proteins of dormant deciduous trees

1998 ◽  
Vol 73 (2-3) ◽  
pp. 165-173 ◽  
Author(s):  
A Golan-Goldhirsh ◽  
A Shachak
1978 ◽  
Vol 171 (2) ◽  
pp. 321-327 ◽  
Author(s):  
J M Bluard-Deconinck ◽  
J Williams ◽  
R W Evans ◽  
J van Snick ◽  
P A Osinski ◽  
...  

Digestion of lactoferrin with pepsin at pH3.0 gave an iron-binding half-molecule that represents the C-terminal part of the native protein. Tryptic or chymotryptic digestion of 30%-iron-saturated lactoferrin yielded the N- and C-terminal half molecules, which could be separated by DEAE-Sephadex chromatography. The N- and C-terminal fragments did not show any immunological cross-reaction. The carbohydrate of lactoferrin was distributed equally between the two fragments.


Virology ◽  
1982 ◽  
Vol 116 (1) ◽  
pp. 382-387 ◽  
Author(s):  
Frank McCormick ◽  
David P. Lane ◽  
Stephen M. Dilworth

1969 ◽  
Vol 43 (4) ◽  
pp. 609-616 ◽  
Author(s):  
ANNE STOCKELL HARTREE ◽  
F. J. CUNNINGHAM

SUMMARY Separation and partial purification of chicken pituitary follicle-stimulating hormone (FSH) and luteinizing hormone (LH) has been obtained by methods which were effective in the purification of the corresponding human and horse hormones. Increases in chicken LH activity were observed after chromatography on DEAE-cellulose and on Amberlite IRC-50 suggesting removal of an LH inhibitor. The biological potencies of chicken FSH and LH preparations when assayed in mammals were very much lower than those of the corresponding mammalian fractions on a weight basis. A weak immunological cross-reaction between chicken and human pituitary LH was used to estimate LH in chicken pituitary fractions and the results were compared with bioassays of the same fractions.


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