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Development of oLH-S-S-gelonin conjugate bearing gelonin on β-subunit of oLH

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Title Development of oLH-S-S-gelonin conjugate bearing gelonin on β-subunit of oLH
 
Creator Singh, Vinod
 
Description 205-209
An attempt was made to cross-link the
βoLH of ovine luteinizing hormone (oLH) to the ribosome inactivating protein, gelonin
in order to develop an effective hormonotoxin for selective targeting to specific
cells in the gonads. Three different molar ratios of oLH and N-succinimidyl-3-(2-pyridyldithio)
propionate (SPDP) were used to activate the epsilon -NH2 groups of
oLH. The βoLH-SPDP derivatives recombine to αoLH and the purified recombinants
retained substantial receptor binding, steroidogenic activity and
immunoreactivity to native oLH. The purified (gel-filtration) βoLH-S-S-gelonin conjugates
were allowed to recombine to αoLH, but an RP-HPLC analysis indicated that
recombination did not take place. The failure to recombine may be due to: (i) the
site of -NH2 activation by SPDP may be different in βoLH from native
oLH; (ii) the activation site may be in close proximity to the recombination site,
which facilitates the recombination of α-subunit but

failed to reassociate to βoLH-S-S-gelonin
conjugate and (iii) the introduction of gelonin (30 kDa basic protein) might
have induced some steric hindrance for αoLH to recombine to the βoLH site which
might have been masked in βoLH-S-Sgelonin conjugates.
 
Date 2013-07-16T08:29:09Z
2013-07-16T08:29:09Z
2000-08
 
Type Article
 
Identifier 0975-0959 (Online); 0301-1208 (Print)
http://hdl.handle.net/123456789/19823
 
Language en_US
 
Rights CC Attribution-Noncommercial-No Derivative Works 2.5 India
 
Publisher NISCAIR-CSIR, India
 
Source IJBB Vol.37(4) [August 2000]