Abstract
A synthetic peptide related to locus adipokinetic hormone (AKH) and shrimp red pigment concentrating hormone (RPCH) containing a tyrosine residue in place of phenylalanine was iodinated and the 3,5-diiodotyrosyl derivative was isolated by reverse phase HPLC. Catalytic dehalogenation of the diiodo derivative in the presence of tritium yielded the tritiated AKH analog which was isolated by gel filtration on Sephadex LH-20 and reverse phase HPLC. The tritiated peptide was formed to be identical to AKH in its ability to stimulate lipid release into the hemolymph of locusts in vivo where the diiodotryrosyl derivative was inactive. The specific radioactivity of the tritiated peptide was 57.2 Ci/mmol, or 99% of the theoretical value.
Muramoto, K;
Ramachandran, J;
Moshitzky, P;
Applebaum, S W
[1]
- Hormone Research Laboratory and Department of Biochemistry and Biophysics, University of California, San Francisco, CA, USA and Department of Entomology, The Hebrew University of Jerusalem, Rehovot, Israel
Citation Formats
Muramoto, K, Ramachandran, J, Moshitzky, P, and Applebaum, S W.
Preparation of a specifically tritiated locust adipokinetic hormone analog with full biological potency.
Denmark: N. p.,
1984.
Web.
Muramoto, K, Ramachandran, J, Moshitzky, P, & Applebaum, S W.
Preparation of a specifically tritiated locust adipokinetic hormone analog with full biological potency.
Denmark.
Muramoto, K, Ramachandran, J, Moshitzky, P, and Applebaum, S W.
1984.
"Preparation of a specifically tritiated locust adipokinetic hormone analog with full biological potency."
Denmark.
@misc{etde_6275192,
title = {Preparation of a specifically tritiated locust adipokinetic hormone analog with full biological potency}
author = {Muramoto, K, Ramachandran, J, Moshitzky, P, and Applebaum, S W}
abstractNote = {A synthetic peptide related to locus adipokinetic hormone (AKH) and shrimp red pigment concentrating hormone (RPCH) containing a tyrosine residue in place of phenylalanine was iodinated and the 3,5-diiodotyrosyl derivative was isolated by reverse phase HPLC. Catalytic dehalogenation of the diiodo derivative in the presence of tritium yielded the tritiated AKH analog which was isolated by gel filtration on Sephadex LH-20 and reverse phase HPLC. The tritiated peptide was formed to be identical to AKH in its ability to stimulate lipid release into the hemolymph of locusts in vivo where the diiodotryrosyl derivative was inactive. The specific radioactivity of the tritiated peptide was 57.2 Ci/mmol, or 99% of the theoretical value.}
journal = []
volume = {23}
journal type = {AC}
place = {Denmark}
year = {1984}
month = {Jan}
}
title = {Preparation of a specifically tritiated locust adipokinetic hormone analog with full biological potency}
author = {Muramoto, K, Ramachandran, J, Moshitzky, P, and Applebaum, S W}
abstractNote = {A synthetic peptide related to locus adipokinetic hormone (AKH) and shrimp red pigment concentrating hormone (RPCH) containing a tyrosine residue in place of phenylalanine was iodinated and the 3,5-diiodotyrosyl derivative was isolated by reverse phase HPLC. Catalytic dehalogenation of the diiodo derivative in the presence of tritium yielded the tritiated AKH analog which was isolated by gel filtration on Sephadex LH-20 and reverse phase HPLC. The tritiated peptide was formed to be identical to AKH in its ability to stimulate lipid release into the hemolymph of locusts in vivo where the diiodotryrosyl derivative was inactive. The specific radioactivity of the tritiated peptide was 57.2 Ci/mmol, or 99% of the theoretical value.}
journal = []
volume = {23}
journal type = {AC}
place = {Denmark}
year = {1984}
month = {Jan}
}