促黑素的酶学研究。
Enzymological studies of melanotropins.
作者信息
Castrucci A M, Hadley M E, Sawyer T K, Hruby V J
出版信息
Comp Biochem Physiol B. 1984;78(3):519-24. doi: 10.1016/0305-0491(84)90090-7.
The relative stability of natural melanotropins and related synthetic analogues to serum and purified proteolytic enzymes was studied. Both alpha- and beta-MSH were rapidly inactivated by frog serum, but much more slowly by rat serum. beta-MSH was more stable than alpha-MSH to serum inactivation. Both alpha- and beta-MSH were rapidly inactivated by alpha-chymotrypsin and trypsin. The synthetic analogues, [Nle4, D-Phe7]-alpha-MSH and [Cys4, Cys10]-alpha-MSH, were totally resistant to inactivation by frog and rat serum enzymes. [Nle4, D-Phe7]-alpha-MSH was resistant to inactivation by alpha-chymotrypsin and trypsin, whereas [Cys4, Cys10]-alpha-MSH was partially resistant to these enzymes under similar conditions. Melanotropin analogues resistant to inactivation by serum enzymes may prove useful in a variety of physiological studies wherein natural melanotropins would be rapidly inactivated.
研究了天然促黑素及相关合成类似物对血清和纯化蛋白水解酶的相对稳定性。α - 促黑素（α - MSH）和β - 促黑素（β - MSH）在蛙血清中均迅速失活，但在大鼠血清中失活速度慢得多。β - MSH对血清失活的稳定性高于α - MSH。α - MSH和β - MSH在α - 胰凝乳蛋白酶和胰蛋白酶作用下均迅速失活。合成类似物[Nle4, D - Phe7] - α - MSH和[Cys4, Cys10] - α - MSH对蛙和大鼠血清酶的失活完全具有抗性。[Nle4, D - Phe7] - α - MSH对α - 胰凝乳蛋白酶和胰蛋白酶的失活具有抗性，而[Cys4, Cys10] - α - MSH在类似条件下对这些酶部分具有抗性。对血清酶失活具有抗性的促黑素类似物在各种天然促黑素会迅速失活的生理学研究中可能证明是有用的。
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