Effect of amino group modification of ovine luteinizing hormone (oLH) by N-succinimidyl 6-[3-(2-pyridyldithio)propionate]hexanoate,a long chain N-succinimidyl-3-(2-pyridyldithio) propionate (SPDP) on immunological and biological properties: a comparative study with SPDP modified oLH |
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Authors: | Vinod Singh Roy Curtiss III |
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Institution: | (1) Institute of Self Organising Systems and Biophysics, North-Eastern Hill University, Permanent Campus, 793 022 Shillong, Meghalaya, India;(2) Department of Biology, Washington University, 63130 St. Louis, Missouri, USA |
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Abstract: | The epsilon-NH2 groups of ovine luteinizing hormone has been modified with the long chain N-succinimidyl-3-(2-pyridyl dithiopropionate (LC-SPDP). The LC-SPDP modification primarily occurs in-NH2 groups of the -subunit. Although, the sequential modification of lysine residue in -subunit led to progressive reduction in the receptor binding and immunological properties but the steroidogenic activity was relatively unaffected. The immunoreactivity and receptor binding properties of LC-SPDP modified oLH molecule were more affected comparative to SPDP modified derivatives. This suggested that the increase in hydrophobic carbon chain in LC-SPDP-oLH molecules resulted into the drastic inhibition in the immunological and biological properties. However, the steroidogenic potential of LC-SPDP/or SPDP-oLH derivative was comparable. The present study clearly demonstrate that a single-NH2 group modification with LC-SPDP would generate the site for the conjugation to the toxin/carrier proteins and the resultant oLH-S-S-toxin conjugate would retain significant immunological and biological properties of the hormone molecule. (Mol Cell Biochem130: 83–90, 1994) |
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Keywords: | Immunoreactivity ovine luteinizing hormone amino group subunits thiolation steroidogenesis receptor binding |
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