Purification and Calcium Dependence of Transglutaminases from Sheep Hair Follicles

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概要

• 論文の詳細を見る

• To study the calcium sensitivity of sheep hair follicle transglutaminase, which was reportedly calcium-independent [H. W. Harding and G. E. Rogers, Biochemistry, 11, 2858-2863 (1972)], the enzyme was purified from a homogenate of merino sheep hair follicles and its calcium dependence was examined. As a result of purification, two types of transglutaminases (DEAE-unabsorbed and absorbed transglutaminase, DU-TG and DA-TG, respectively) were obtained. The molecular mass of DU-TG was 77 and 82 kDa by SDS-PAGE and gel filtration, respectively, while that of DA-TG was 40 and 80 kDa. Each enzyme was obviously calcium dependent and contained (a) cysteine residue(s) in the active site, like other known mammalian transglutaminases. Maximum activation of DU-TG and DA-TG was observed at 1 and 0.1 mM CaCl_2, respectively.

• 社団法人日本農芸化学会の論文
• 1997-07-23

著者

• Ohtsuka Tomoko

  Ajinomoto Co. Inc. Food Development & Research Laboratories

• Seguro K

  Ajinomoto Co. Inc. Kanagawa Jpn

• KUMAZAWA Yoshiyuki

  Ajinomoto Co., Inc., Food Development & Research Laboratories

• NINOMIYA Daiki

  Ajinomoto Co., Inc., Food Development & Research Laboratories

• SEGURO Katsuya

  Ajinomoto Co., Inc., Food Development & Research Laboratories

• Ninomiya Daiki

  Ajinomoto Co. Inc. Food Development & Research Laboratories

• Kumazawa Yoshiyuki

  Ajinomoto Co. Inc. Food Development & Research Laboratories

関連論文

• Immobilization of Enzyme in Protein Films Prepared Using Transglutaminase(Food & Nutrition)
• α_-Casein Film Prepared Using Transglutaminase(Food & Nutrition)
• Glutamine-specific Deamidation of α_-Casein by Transglutaminase(Food & Nutrition)
• Purification and Calcium Dependence of Transglutaminases from Sheep Hair Follicles

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