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 α-subunit. Although, the sequential modification of lysine residue in α-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 Biochem 130: 83-90, 1994)
Original language | English (US) |
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Pages (from-to) | 83-90 |
Number of pages | 8 |
Journal | Molecular and Cellular Biochemistry |
Volume | 130 |
Issue number | 1 |
DOIs | |
State | Published - Jan 1994 |
Externally published | Yes |
Keywords
- Immunoreactivity, ovine luteinizing hormone
- amino group
- receptor binding
- steroidogenesis
- subunits
- thiolation
ASJC Scopus subject areas
- Molecular Biology
- Clinical Biochemistry
- Cell Biology