Purification and amino acid sequence of kunitz-type protease inhibitor found in the hemocytes of horseshoe crab (Tachypleus tridentatus)

Takanori Nakamura, Toshiaki Hirai, Fuminori Tokunaga, Shun-Ichiro Kawabata, Sadaaki Iwanaga

研究成果: ジャーナルへの寄稿記事

30 引用 (Scopus)

抄録

A low molecular weight protein protease inhibitor was purified from Japanese horseshoe crab (Tachypleus tridentatus) hemocytes. It consisted of a single polypeptide with a total of 61 amino acid residues. This protease inhibitor inhibited stoichiometrically the amidase activity of trypsin (K1=4.60×10-10 M), and also had inhibitory effects on α-chymotrypsin (K1=5.54×10-9M), elastase (K1=7.20×10-8 M), plasmin, and plasma kallikrein. However, it had no effect on T. tridentatus clotting enzyme and factor C, mammalian blood coagulation factors (activated protein C, factor Xa and α-thrombin), papain, and thermolysin. The complete amino acid sequence of this inhibitor was determined and its sequence was compared with those of bovine pancreatic trypsin inhibitor (BPTI) and other Kunitz-type inhibitors. It was found that the amino acid sequence of this inhibitor has a high homology of 47 and 43% with those of sea anemone inhibitor 5-II and BPTI, respectively. Thus, this protease inhibitor appeared to be one of the typical Kunitz-type protease inhibitors.

元の言語英語
ページ(範囲)1297-1306
ページ数10
ジャーナルJournal of biochemistry
101
発行部数5
DOI
出版物ステータス出版済み - 1 1 1987

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Horseshoe Crabs
Hemocytes
Protease Inhibitors
Purification
Amino Acid Sequence
Amino Acids
Aprotinin
Blood Coagulation Factors
amidase
Plasma Kallikrein
Sea Anemones
Thermolysin
Factor Xa
Papain
Pancreatic Elastase
Fibrinolysin
Chymotrypsin
Protein C
Thrombin
Trypsin

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology

これを引用

Purification and amino acid sequence of kunitz-type protease inhibitor found in the hemocytes of horseshoe crab (Tachypleus tridentatus). / Nakamura, Takanori; Hirai, Toshiaki; Tokunaga, Fuminori; Kawabata, Shun-Ichiro; Iwanaga, Sadaaki.

:: Journal of biochemistry, 巻 101, 番号 5, 01.01.1987, p. 1297-1306.

研究成果: ジャーナルへの寄稿記事

Nakamura, Takanori ; Hirai, Toshiaki ; Tokunaga, Fuminori ; Kawabata, Shun-Ichiro ; Iwanaga, Sadaaki. / Purification and amino acid sequence of kunitz-type protease inhibitor found in the hemocytes of horseshoe crab (Tachypleus tridentatus). :: Journal of biochemistry. 1987 ; 巻 101, 番号 5. pp. 1297-1306.
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abstract = "A low molecular weight protein protease inhibitor was purified from Japanese horseshoe crab (Tachypleus tridentatus) hemocytes. It consisted of a single polypeptide with a total of 61 amino acid residues. This protease inhibitor inhibited stoichiometrically the amidase activity of trypsin (K1=4.60×10-10 M), and also had inhibitory effects on α-chymotrypsin (K1=5.54×10-9M), elastase (K1=7.20×10-8 M), plasmin, and plasma kallikrein. However, it had no effect on T. tridentatus clotting enzyme and factor C, mammalian blood coagulation factors (activated protein C, factor Xa and α-thrombin), papain, and thermolysin. The complete amino acid sequence of this inhibitor was determined and its sequence was compared with those of bovine pancreatic trypsin inhibitor (BPTI) and other Kunitz-type inhibitors. It was found that the amino acid sequence of this inhibitor has a high homology of 47 and 43{\%} with those of sea anemone inhibitor 5-II and BPTI, respectively. Thus, this protease inhibitor appeared to be one of the typical Kunitz-type protease inhibitors.",
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