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

Yasuhiro Kohama; Masaru Okabe; Kazutake Tsujikawa; Hiroaki Oka; Tetsuyuki Teramoto; Yuzo Kayamori; Masaaki Itoh; 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, Masaru Okabe, Kazutake Tsujikawa, Hiroaki Oka, Tetsuyuki Teramoto, Yuzo Kayamori, Masaaki Itoh, 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 radiactivity, was found to be biologically active in the BALB/c 3Ts 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 Try-24 and Try-60. This is the first report of the biological activity of radioactive peptide hormone with a defined laveled 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

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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 radiactivity, was found to be biologically active in the BALB/c 3Ts 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 Try-24 and Try-60. This is the first report of the biological activity of radioactive peptide hormone with a defined laveled site.",

author = "Yasuhiro Kohama and Masaru Okabe and Kazutake Tsujikawa and Hiroaki Oka and Tetsuyuki Teramoto and Yuzo Kayamori and Masaaki Itoh and Tsutomu Mimura",

year = "1992",

doi = "10.1248/cpb.40.808",

language = "English",

volume = "40",

pages = "808--810",

journal = "Chemical and Pharmaceutical Bulletin",

issn = "0009-2363",

publisher = "The Pharmaceutical Society of Japan",

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TY - JOUR

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

AU - Kohama, Yasuhiro

AU - Okabe, Masaru

AU - Tsujikawa, Kazutake

AU - Oka, Hiroaki

AU - Teramoto, Tetsuyuki

AU - Kayamori, Yuzo

AU - Itoh, Masaaki

AU - Mimura, Tsutomu

PY - 1992

Y1 - 1992

N2 - 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 radiactivity, was found to be biologically active in the BALB/c 3Ts 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 Try-24 and Try-60. This is the first report of the biological activity of radioactive peptide hormone with a defined laveled site.

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 radiactivity, was found to be biologically active in the BALB/c 3Ts 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 Try-24 and Try-60. This is the first report of the biological activity of radioactive peptide hormone with a defined laveled site.

U2 - 10.1248/cpb.40.808

DO - 10.1248/cpb.40.808

M3 - Article

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VL - 40

SP - 808

EP - 810

JO - Chemical and Pharmaceutical Bulletin

JF - Chemical and Pharmaceutical Bulletin

IS - 3

ER -

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

Abstract

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