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Biochimica et Biophysica Acta | 1979

Occurrence of Leu-Lys-bradykinin and histidine-rich peptide in high-molecular-weight kininogen isolated from horse plasma

Teruko Sugo; Hisao Kato; Sadaaki Iwanaga; Setsuro Fujii

On incubation of purified horse plasma high-molecular-weight kininogen with purified plasma kallikrein, three new peptides, named fragment 1.2, fragment 1 and fragment 2, were released, in addition to the vasopeptide, bradykinin. Fragment 2 contained an extremely high level of histidine, in which eleven residues out of the total 48 residues were characterized. Thus the result proves the existence of the histidine-rich region in horse high-molecular-weight kininogen, which is similar to the region previously identified in bovine high-molecular-weight kininogen. Moreover, we have identified a new kinin derivative, Leu-Lys-bradykinin, in horse high-molecular-weight kininogen.


Archive | 1979

The Kallikrein-Kinin System: A Functional Role of Plasma Kallikrein and Kininogen in Blood Coagulation

Sadaaki Iwanaga; Hisao Kato; Teruko Sugo; Nobuhiko Ikari; N. Hashimoto; Setsuro Fujii

Bradykinin is a nonapeptide with potent pharmacological activities such as smooth muscle contraction and hypotension. In mammalian plasma, this physiologically active peptide is in precursor form, called kininogen, and liberated by the action of specific enzyme, plasma kallikrein, or tissue kallikreins. Bovine plasma contains at least two kininogens, named high molecular weight (HMW) kininogen and low molecular weight (LMW) kininogen (Yano et al., 1967). In Figure 1, the linear polypeptide sequences of kininogens are shown for comparison. The areas of which amino acid sequence has been established are indicated by shaded areas. HMW kininogen consists of a single chain with a molecular weight of 76,000, containing four segments, heavy chain, the kinin moiety, fragment 1·2 and light chain (Han et al., 1976). It contains 580 amino acid residues and 12.5% carbohydrates. This kininogen is the physiological substrate of plasma kallikrein (Yano et al., 1971). LMW kininogen, on the other hand, has a molecular weight of 48,000. It consists of 380 residues and 16.4% carbohydrate (Kato et al., 1976).


Thrombosis and Haemostasis | 1995

Calcium ion-dependent monoclonal antibody against human fibrinogen: preparation, characterization, and application to fibrinogen purification.

Mikihiro Takebe; Gilbu Soe; Isao Kohno; Teruko Sugo; Michio Matsuda


Biochemistry | 1980

Functional sites of bovine high molecular weight kininogen as a cofactor in kaolin-mediated activation of factor XII (Hageman factor)

Teruko Sugo; Nobuhiko Ikari; Hisao Kato; Sadaaki Iwanaga; Setsuro Fujii


Blood | 1999

Fibrinogen Niigata With Impaired Fibrin Assembly: An Inherited Dysfibrinogen With a Bβ Asn-160 to Ser Substitution Associated With Extra Glycosylation at Bβ Asn-158

Teruko Sugo; Chizuko Nakamikawa; Hiroshi Takano; Jun Mimuro; Shu-ichi Yamaguchi; Michael W. Mosesson; David A. Meh; James P. DiOrio; Noriko Takahashi; Hoyu Takahashi; Koichi Nagai; Michio Matsuda


Blood | 2004

Thrombophilic dysfibrinogen Tokyo V with the amino acid substitution of γ ALa327thr: formation of fragile but fibrinolysis-resistant fibrin clots and its relevance to arterial thromboembolism

Akiei Hamano; Jun Mimuro; Motonori Aoshima; Takeyoshi Itoh; Noboru Kitamura; Susumu Nishinarita; Katsuhiro Takano; Akira Ishiwata; Yuji Kashiwakura; Kazuki Niwa; Tomoko Ono; Seiji Madoiwa; Teruko Sugo; Michio Matsuda; Yoichi Sakata


International Journal of Hematology | 1993

Flow cytometric analysis of surface membrane proteins on activated platelets and platelet-derived microparticles from healthy and thrombasthenic individuals.

Shosaku Nomura; Yutaka Komiyama; Murakami T; Funatsu A; Kokawa T; Teruko Sugo; Michio Matsuda; Yasunaga K


FEBS Journal | 2005

High‐Molecular‐Weight Kininogen from Horse Plasma

Teruko Sugo; Setsuro Fujii; Hisao Kato; Sadaaki Iwanaga


Thrombosis and Haemostasis | 2002

Substitution of Gly-548 to Ala in the substrate binding pocket of prothrombin Perijá leads to the loss of thrombin proteolytic activity.

Osamu Sekine; Teruko Sugo; Kazuyoshi Ebisawa; Hideaki Umeyama; Hiroyuki Iwahana; Arlette Ruiz-Saez; Norma B. de Bosch; Michio Matsuda


Journal of Biochemistry | 1982

A Method for Preparation of a Single Chain High-Molecular-Weight(HMW) Kininogen from Bovine Plasma

Toshio Shimada; Teruko Sugo; Hisao Kato; Sadaaki Iwanaga

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Michio Matsuda

Jikei University School of Medicine

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Jun Mimuro

Jichi Medical University

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Akira Ishiwata

Jichi Medical University

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