Purification and Characterization of a Tissue-type Transglutaminase from Red Sea Bream (Pagrus major)
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概要
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A tissue-type transglutaminase (TGase) was purified from liver tissue of the red sea bream, Pagrus major, by ion-exchange chromatography and heparin-Sepharose affinity chromatography. Its activity was assessed using a fluorometric assay to measure the incorporation of monodansylcadaverine into N, N'-dimethyl casein. The molecular mass of purified TGase was estimated to be 78kDa by SDS-polyacrylamide gel electrophoresis. The enzyme required Ca^<2+> to express its activity, although 10 mM Sr^<2+> also activated the enzyme fully. TGase activity was maximal at pH 9.0-9.5, and the enzyme was strongly inhibited by sulfhydryl reagents. The purified enzyme catalyzed the cross-linking of myosin heavy chain obtained from Alaska pollack, resulting in gelation of an actomyosin solution. The partial amino acid sequence of this fish TGase showed divisionally significant similarity to TGase from guinea pig liver.
- 1994-11-23
著者
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MOTOKI Masao
Food Research & Development Laboratories, Ajinomoto Co., Inc.
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Motoki M
Ajinomoto Co. Inc. Kawasaki Jpn
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KUMAZAWA Yoshiyuki
Food Research and Development Laboratories, Ajinomoto Co., Inc.
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YASUEDA Hisashi
Food Research and Development Laboratories, Ajinomoto Co., Inc.
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Yasuda H
Obihiro Univ. Agriculture And Veterinary Medicine Hokkaido Jpn
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Kumazawa Y
Ajinomoto Co. Inc. Kawasaki‐shi Jpn
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Kumazawa Yoshiyuki
Food Research And Development Laboratories Ajinomoto Co. Inc.
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