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核心技术专利：CN118964589B侵权必究

核心技术专利：CN118964589B侵权必究

Gráf L, Barát E, Borvendég J, Hermann I, Patthy A

Eur J Biochem. 1976 May 1;64(2):333-40. doi: 10.1111/j.1432-1033.1976.tb10306.x.

This communication reports the action of bovine thrombin on ovine, bovine and human growth hormones. Thrombin cleavage was shown to be restricted to a single homologous peptide bond in all three growth hormones (at sequence positions 133--134 of the ovine and bovine hormones). 2. Ovine growth hormone was the most sensitive to the action of thrombin, bovine growth hormone was attacked to a relatively less extent, and human growth hormone was the most resistant to the enzyme. 3. After reduction and carbamidomethylation of the disulfide bonds in thrombin modified ovine growth hormone, the two fragments (residues 1--133 and 134--191) were isolated. The large NH2-terminal thrombin fragment of the hormone (residues 1--133) was found to be inactive in the rat tibia test, whereas a tryptic fragment (residues 96--133) isolated in an independent way gave measurable responses.

本通讯报道了牛凝血酶对绵羊、牛和人生长激素的作用。已表明凝血酶切割仅限于所有三种生长激素中的一个同源肽键（在绵羊和牛激素的序列位置133 - 134处）。2. 绵羊生长激素对凝血酶的作用最敏感，牛生长激素受到的影响相对较小，而人生长激素对该酶最具抗性。3. 在对凝血酶修饰的绵羊生长激素中的二硫键进行还原和氨甲酰甲基化后，分离出两个片段（残基1 - 133和134 - 191）。发现该激素的大的NH2末端凝血酶片段（残基1 - 133）在大鼠胫骨试验中无活性，而以独立方式分离的胰蛋白酶片段（残基96 - 133）产生了可测量的反应。

Gráf L, Barát E, Borvendég J, Hermann I, Patthy A

Eur J Biochem. 1976 May 1;64(2):333-40. doi: 10.1111/j.1432-1033.1976.tb10306.x.

This communication reports the action of bovine thrombin on ovine, bovine and human growth hormones. Thrombin cleavage was shown to be restricted to a single homologous peptide bond in all three growth hormones (at sequence positions 133--134 of the ovine and bovine hormones). 2. Ovine growth hormone was the most sensitive to the action of thrombin, bovine growth hormone was attacked to a relatively less extent, and human growth hormone was the most resistant to the enzyme. 3. After reduction and carbamidomethylation of the disulfide bonds in thrombin modified ovine growth hormone, the two fragments (residues 1--133 and 134--191) were isolated. The large NH2-terminal thrombin fragment of the hormone (residues 1--133) was found to be inactive in the rat tibia test, whereas a tryptic fragment (residues 96--133) isolated in an independent way gave measurable responses.

本通讯报道了牛凝血酶对绵羊、牛和人生长激素的作用。已表明凝血酶切割仅限于所有三种生长激素中的一个同源肽键（在绵羊和牛激素的序列位置133 - 134处）。2. 绵羊生长激素对凝血酶的作用最敏感，牛生长激素受到的影响相对较小，而人生长激素对该酶最具抗性。3. 在对凝血酶修饰的绵羊生长激素中的二硫键进行还原和氨甲酰甲基化后，分离出两个片段（残基1 - 133和134 - 191）。发现该激素的大的NH2末端凝血酶片段（残基1 - 133）在大鼠胫骨试验中无活性，而以独立方式分离的胰蛋白酶片段（残基96 - 133）产生了可测量的反应。