Studies on the iodination of LH-RH and the biological and immunological activities of the products

P. Piyachaturawata; E. Pedroza; W. Y. Huang; A. Arimura; A. V. Schally

doi:10.1016/0024-3205(80)90090-9

Studies on the iodination of LH-RH and the biological and immunological activities of the products

P. Piyachaturawata, E. Pedroza, W. Y. Huang, A. Arimura, A. V. Schally

Research output: Contribution to journal › Article › peer-review

8 Scopus citations

Abstract

Synthetic LH-RH was iodinated by the modified chloramine-T or lactoperoxidase method, using ¹²⁷INa or ¹²⁵INa. The yields of the products, the LH releasing activities of the monoiodinated peptides as well as binding to pituitary membrane fractions were measured. The variation in yield in the four procedures used for iodination was a function of the amount of oxidizing agent. Monoiodinated products obtained by the different procedures possessed comparable LH-releasing activities as well as binding affinity to pituitary plasma membranes.

Original language	English (US)
Pages (from-to)	1309-1318
Number of pages	10
Journal	Life Sciences
Volume	26
Issue number	16
DOIs	https://doi.org/10.1016/0024-3205(80)90090-9
State	Published - Apr 21 1980
Externally published	Yes

ASJC Scopus subject areas

Biochemistry, Genetics and Molecular Biology(all)
Pharmacology, Toxicology and Pharmaceutics(all)

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10.1016/0024-3205(80)90090-9

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title = "Studies on the iodination of LH-RH and the biological and immunological activities of the products",

abstract = "Synthetic LH-RH was iodinated by the modified chloramine-T or lactoperoxidase method, using 127INa or 125INa. The yields of the products, the LH releasing activities of the monoiodinated peptides as well as binding to pituitary membrane fractions were measured. The variation in yield in the four procedures used for iodination was a function of the amount of oxidizing agent. Monoiodinated products obtained by the different procedures possessed comparable LH-releasing activities as well as binding affinity to pituitary plasma membranes.",

author = "P. Piyachaturawata and E. Pedroza and Huang, {W. Y.} and A. Arimura and Schally, {A. V.}",

note = "Funding Information: ~hese studies were supported in part by NICHHD Contract HD-8-2819, NIH grant AM 07467 and the Veterans Administration. Funding Information: Dr. p. Piyachaturawat a held course of this investigation a fellowship from the Rockefeller Foundation in the (Post-doctoral trainee).",

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doi = "10.1016/0024-3205(80)90090-9",

language = "English (US)",

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pages = "1309--1318",

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T1 - Studies on the iodination of LH-RH and the biological and immunological activities of the products

AU - Piyachaturawata, P.

AU - Pedroza, E.

AU - Huang, W. Y.

AU - Arimura, A.

AU - Schally, A. V.

N1 - Funding Information: ~hese studies were supported in part by NICHHD Contract HD-8-2819, NIH grant AM 07467 and the Veterans Administration. Funding Information: Dr. p. Piyachaturawat a held course of this investigation a fellowship from the Rockefeller Foundation in the (Post-doctoral trainee).

PY - 1980/4/21

Y1 - 1980/4/21

N2 - Synthetic LH-RH was iodinated by the modified chloramine-T or lactoperoxidase method, using 127INa or 125INa. The yields of the products, the LH releasing activities of the monoiodinated peptides as well as binding to pituitary membrane fractions were measured. The variation in yield in the four procedures used for iodination was a function of the amount of oxidizing agent. Monoiodinated products obtained by the different procedures possessed comparable LH-releasing activities as well as binding affinity to pituitary plasma membranes.

AB - Synthetic LH-RH was iodinated by the modified chloramine-T or lactoperoxidase method, using 127INa or 125INa. The yields of the products, the LH releasing activities of the monoiodinated peptides as well as binding to pituitary membrane fractions were measured. The variation in yield in the four procedures used for iodination was a function of the amount of oxidizing agent. Monoiodinated products obtained by the different procedures possessed comparable LH-releasing activities as well as binding affinity to pituitary plasma membranes.

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