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

Vinod Singh, Roy Curtiss

Research output: Contribution to journalArticle

6 Citations (Scopus)

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 languageEnglish (US)
Pages (from-to)83-90
Number of pages8
JournalMolecular and Cellular Biochemistry
Volume130
Issue number1
DOIs
StatePublished - Jan 1994
Externally publishedYes

Fingerprint

Propionates
Luteinizing Hormone
Sheep
Immunotoxins
Molecules
Immunologic Receptors
Derivatives
Lysine
Carrier Proteins
Carbon
N-succinimidyl 3-(2-pyridyldithio)propionate
hexanoic acid
Hormones

Keywords

  • amino group
  • Immunoreactivity, ovine luteinizing hormone
  • receptor binding
  • steroidogenesis
  • subunits
  • thiolation

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics
  • Clinical Biochemistry
  • Cell Biology

Cite this

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title = "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",
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)",
keywords = "amino group, Immunoreactivity, ovine luteinizing hormone, receptor binding, steroidogenesis, subunits, thiolation",
author = "Vinod Singh and Roy Curtiss",
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TY - JOUR

T1 - 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

T2 - a comparative study with SPDP modified oLH

AU - Singh, Vinod

AU - Curtiss, Roy

PY - 1994/1

Y1 - 1994/1

N2 - 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)

AB - 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)

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