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Title: Modification of ovine luteinizing hormone subunits with SMPT and its effect on subunit recombination, immunological activity, receptor binding and steroidogenic activity
Authors: Singh, Vinod
Singh, Ranjit C
Issue Date: Sep-1999
Publisher: NISCAIR-CSIR, India
Abstract: The increasing use of heterobifunctional cross-linking agents in the design of defined conjugates for selective targeting and inducing immune response has prompted us to study the role of ε-NH2 group modification of oLH subunits, their recombination and effect on immunoreactivity, receptor binding and biological activity. The ε-N H2 groups of o:oLH and αoLH subunits were separately modified by using SMPT. The αoLH-SMPT modified derivatives hybridize to βoLH Similarly, the βoLH-SMPT derivatives recombined with αoLH. The recombination was judged by gel filtration chromatography and RP-HPLC analysis. The sequential modification of subunits led to progressive reduction in immunoreactivity and receptor binding activity. The modification of six or more ε-NH2 groups in αoLH although recombine fully with native βoLH but failed to react to anti-oLH antibody. Moreover, the steroidogenic activity was also abolished. Introduction upto four SMPT groups in αoLH compromised immunological and biological activities but further addition of two or more SMPT groups completely abolished antibody reactivity, receptor binding and steroidogenic activity indicating the importance of later two amino groups in the receptor binding and steroidogenic activity. The present investigation clearly demonstrate that only 1:2-3 molar ratio of oLH subunits:SMPT could generate the site(s) in the subunits of the oLH that retained reasonable immunological , receptor binding and biological activity of the hormone. Therefore, this molar ratio may be used in future for the design and synthesis of bio effective hormonotoxins.
Page(s): 849-858
ISSN: 0975-1009 (Online); 0019-5189 (Print)
Appears in Collections: IJEB Vol.37(09) [September 1999]

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