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서양고추냉이 Peroxidase 의 염기성 Isozyme 의 아미노산 배열에 관한 연구 KCI 등재

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한국식품영양학회지 (The Korean Journal of Food And Nutrition)
한국식품영양학회 (The Korean Society of Food and Nutrition)
초록

The amino acid sequence of basic isozyme E5 of Horseradish Peroxidase(HRP E5) was determined by protein sequencing. HRP E5 consisted about 300 residues, and has a molecular weight of approximately 36, 000±500 dalton. The protein was rich in aspartic acid (14%), arginine (13%), and leucine(ll%). The primary structure of HRP E5 was established by sequencing its tryptic(T_1-T_19) and lysylendopeptic(A_1-A_3) peptides. The sequence homology between HRP E5 and HRP C(neutral isozyme of horseradish peroxidase) is found to be more than 66%. The highest concentration of identical residues are found on residues 29∼56, 90∼123, and 155∼173, but relatively low on 174∼271.

저자
  • 소명환 | Myung Hwan So
  • 조신호 | Shin Ho Cho
  • 윤성식 | Sung Sik Yoon
  • 남궁석 | Sok Namkung