Preparation of Biologically Active and Site Specifically Radioiodinated Recombinant Human Insulin-like Growth Factor-I

Yasuhiro Kohama; Ma Sar U. Okabe; Kazutake Tsujikawa; Hiroaki Oka; Tetsuyuki Teramoto; Yuzo Kayamor; M. Masaaki; Tsutomu Mimura

doi:10.1248/cpb.40.808

Preparation of Biologically Active and Site Specifically Radioiodinated Recombinant Human Insulin-like Growth Factor-I

Yasuhiro Kohama, Ma Sar U. Okabe, Kazutake Tsujikawa, Hiroaki Oka, Tetsuyuki Teramoto, Yuzo Kayamor, M. Masaaki, Tsutomu Mimura

Division of Medical Technology

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

Abstract

Recombinant human insulin-like growth factor-I (rhIGF-I) was iodinated using a lactoperoxidase-catalyzed labeling method. The labeled products were separated into more than five fractions by ion-paired reverse-phase high performance liquid chromatography (HPLC). A fraction (peak 1), which showed the highest yield and radioactivity, was found to be biologically active in the BALB/c 3T3 cell proliferating system. The site of the iodination was investigated by S-pyridylethylation followed by trypsinization and separation with HPLC using reverse phase columns. From the amino acid analysis of the peaks which were radioactive, the iodination site of peak 1 was revealed to be Tyr-24 and Tyr-60. This is the first report of the biological activity of radioactive peptide hormone with a defined labeled site.

Original language	English
Pages (from-to)	808-810
Number of pages	3
Journal	Chemical and Pharmaceutical Bulletin
Volume	40
Issue number	3
DOIs	https://doi.org/10.1248/cpb.40.808
Publication status	Published - 1992

All Science Journal Classification (ASJC) codes

Chemistry(all)
Drug Discovery

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title = "Preparation of Biologically Active and Site Specifically Radioiodinated Recombinant Human Insulin-like Growth Factor-I",

abstract = "Recombinant human insulin-like growth factor-I (rhIGF-I) was iodinated using a lactoperoxidase-catalyzed labeling method. The labeled products were separated into more than five fractions by ion-paired reverse-phase high performance liquid chromatography (HPLC). A fraction (peak 1), which showed the highest yield and radioactivity, was found to be biologically active in the BALB/c 3T3 cell proliferating system. The site of the iodination was investigated by S-pyridylethylation followed by trypsinization and separation with HPLC using reverse phase columns. From the amino acid analysis of the peaks which were radioactive, the iodination site of peak 1 was revealed to be Tyr-24 and Tyr-60. This is the first report of the biological activity of radioactive peptide hormone with a defined labeled site.",

author = "Yasuhiro Kohama and Okabe, {Ma Sar U.} and Kazutake Tsujikawa and Hiroaki Oka and Tetsuyuki Teramoto and Yuzo Kayamor and M. Masaaki and Tsutomu Mimura",

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T1 - Preparation of Biologically Active and Site Specifically Radioiodinated Recombinant Human Insulin-like Growth Factor-I

AU - Kohama, Yasuhiro

AU - Okabe, Ma Sar U.

AU - Tsujikawa, Kazutake

AU - Oka, Hiroaki

AU - Teramoto, Tetsuyuki

AU - Kayamor, Yuzo

AU - Masaaki, M.

AU - Mimura, Tsutomu

PY - 1992

Y1 - 1992

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AB - Recombinant human insulin-like growth factor-I (rhIGF-I) was iodinated using a lactoperoxidase-catalyzed labeling method. The labeled products were separated into more than five fractions by ion-paired reverse-phase high performance liquid chromatography (HPLC). A fraction (peak 1), which showed the highest yield and radioactivity, was found to be biologically active in the BALB/c 3T3 cell proliferating system. The site of the iodination was investigated by S-pyridylethylation followed by trypsinization and separation with HPLC using reverse phase columns. From the amino acid analysis of the peaks which were radioactive, the iodination site of peak 1 was revealed to be Tyr-24 and Tyr-60. This is the first report of the biological activity of radioactive peptide hormone with a defined labeled site.

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Preparation of Biologically Active and Site Specifically Radioiodinated Recombinant Human Insulin-like Growth Factor-I

Abstract

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