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鸡胚中组氨酸和鸟氨酸的脱羧酶

Decarboxylases of histidine and ornithine in chick embryo.

作者信息

Dzodzoe Y C, Rosengren E

出版信息

Br J Pharmacol. 1971 Feb;41(2):294-301. doi: 10.1111/j.1476-5381.1971.tb08030.x.

Abstract
  1. The activities of histidine and ornithine decarboxylases as well as the histamine content of the developing chick embryo were studied.2. Histidine decarboxylase (L-histidine carboxy-lyase; E.C. 4.1.1.22) activity was fairly low with a tendency to increase at later stages of development. This enzyme was preferentially present in the supernatant fraction of the tissue homogenate. alpha-Methyl-histidine, but not alpha-methyl-DOPA, inhibited its activity.3. The histamine content per gramme of embryo was low with a tendency to increase with the age of the embryo.4. Ornithine decarboxylase (L-ornithine carboxy-lyase; E.C. 4.1.1.17) activity was high at the beginning of the stages of development investigated, but later there was a steep fall in activity. A noticeable feature was that while the activity in the residual fraction of the homogenate remained almost constant during development, the activity in the supernatant fraction was high in the early stages, then fell rapidly to nearly zero at later stages.
摘要
  1. 对发育中的鸡胚中组氨酸脱羧酶和鸟氨酸脱羧酶的活性以及组胺含量进行了研究。

  2. 组氨酸脱羧酶(L-组氨酸羧基裂解酶;E.C. 4.1.1.22)活性相当低,在发育后期有增加的趋势。该酶优先存在于组织匀浆的上清液部分。α-甲基组氨酸而非α-甲基多巴可抑制其活性。

  3. 每克胚体中的组胺含量较低,且有随胚龄增加的趋势。

  4. 鸟氨酸脱羧酶(L-鸟氨酸羧基裂解酶;E.C. 4.1.1.17)活性在所研究的发育阶段开始时较高,但随后活性急剧下降。一个显著特点是,虽然匀浆残余部分的活性在发育过程中几乎保持不变,但上清液部分的活性在早期较高,随后在后期迅速降至几乎为零。

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Decarboxylases of histidine and ornithine in chick embryo.鸡胚中组氨酸和鸟氨酸的脱羧酶
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Radiometric micromethods for the study of some amino acid decarboxylases.
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本文引用的文献

1
The quantitative estimation of histamine in the blood.血液中组胺的定量测定。
J Physiol. 1937 Apr 9;89(3):257-68. doi: 10.1113/jphysiol.1937.sp003476.
5
OBSERVATIONS ON THE INHIBITION OF HISTAMINE FORMATION.关于组胺形成抑制的观察
J Physiol. 1963 Dec;169(3):467-86. doi: 10.1113/jphysiol.1963.sp007273.
9
Formation and binding of histamine by rat tissues in vitro.大鼠组织在体外对组胺的形成与结合
Am J Physiol. 1956 Sep;187(1):63-5. doi: 10.1152/ajplegacy.1956.187.1.63.
10

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