MEI-YU XIE

Chinese Academy of Medical Sciences & Peking Union Medical College

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TOSHIO OTANI

Komatsu (Japan)

Teruyoshi Marunaka

Taiho Pharmaceutical (Japan)

Yoshinori Minami

Asahikawa Medical University

Rui Zhang

Sixth Affiliated Hospital of Xinjiang Medical University

Yuji Yamada

Tokyo University of Pharmacy and Life Sciences

Tie Tian

Wuhan Polytechnic University

Ichiro Yamawaki

Taiho Pharmaceutical (Japan)

Tadashi Yasuhara

Kitasato University

CHANG-QING Qi

Chinese Academy of Medical Sciences & Peking Union Medical College

Rui Zhang

Harbin Normal University

Cooperative Institutions

Chinese Academy of Medical Sciences & Peking Union Medical College

Taiho Pharmaceutical (Japan)

Tokushima University

Kunming Institute of Botany

Tohoku University

Academy of Medical Sciences

Tamagawa University

Wuhan Polytechnic University

Jilin University

State Key Laboratory of Automotive Simulation and Control

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C-1027-AG, a selective antagonist of the macromolecular antitumor antibiotic, C-1027.

The Journal of Antibiotics (1988)

TOSHIO OTANI Yoshinori Minami Teruyoshi Marunaka Rui Zhang MEI-YU XIE

10.7164/antibiotics.41.1696

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Citations (8)

Purification and primary structure of C-1027-AG, a selective antagonist of antitumor antibiotic C-1027, from Streptomyces globisporus.

Agricultural and Biological Chemistry (1991)

TOSHIO OTANI Tadashi Yasuhara Yoshinori Minami Tsuneo SHIMAZU Rui Zhang

C-1027-AG, a selective antagonist of antitumor antibiotic C-1027, was isolated by column chromatography on DEAE-cellulose, butyl-Toyopearl and Sephadex G-50 from a culture filtrate of Streptomyces globisporus. The amino acid sequence of purified C-1027-AG was determined with a protein sequencer on the basis of fragment peptides obtained by enzymatic hydrolysis with lysylendopeptidase, V8 protease, endopeptidase AspN and chymotrypsin, after performic acid oxidation. C-1027-AG is shown to consist of a single polypeptide chain cross-linked by two disulfide bonds, and to contain a total of 110 amino acid residues with alanine and glycine as its amino- and carboxyl-termini, respectively; its molecular weight was calculated to be 10, 500 daltons. The primary structure of C-1027-AG is indicated to be identical to the protein moiety of C-1027, and is highly homologous to the sequences of antitumor proteins obtained from other Streptomyces species.

Performic acid

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Sephadex

Protein primary structure

Alanine

10.1271/bbb1961.55.407

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Citations (17)

A new macromolecular antitumor antibiotic, C-1027. II. Isolation and physico-chemical properties.

The Journal of Antibiotics (1988)

TOSHIO OTANI Yoshinori Minami Teruyoshi Marunaka Rui Zhang MEI-YU XIE

Sephadex