Phân tích tư tưởng của nhân dân qua đoạn thơ: Những người vợ nhớ chồng… Những cuộc đời đã hóa sông núi ta trong Đất nước của Nguyễn Khoa Điềm
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The thermal unfoldingofmyosinsubfragment 1 (S1) cleavedby trypsin was studied by differential scanning calorimetry.In the absence of nucleotides, trypsin splits the S1 heavychain into three fragments (25, 50, and 20 kDa). Thiscleavage has no appreciable influence on the thermalunfolding of S1 examined in the presence of ADP, in theternary complexes of S1 with ADP and phosphate analogs,such as orthovanadate (Vi) or berylliumfluoride (BeFx), andin the presence of F-actin.
Nội dung trích xuất từ tài liệu:
Báo cáo Y học: Differential scanning calorimetric study of myosin subfragment 1 with tryptic cleavage at the N-terminal region of the heavy chain
