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人胆汁和胆道黏膜中的激肽形成与破坏活性。

Kinin forming and destroying activities in human bile and mucous membranes of the biliary tract.

作者信息

Nielsen H M

出版信息

Br J Pharmacol. 1969 Sep;37(1):172-7. doi: 10.1111/j.1476-5381.1969.tb09535.x.

Abstract
  1. Human bile and tissue homogenates from the mucous membranes of the biliary tract possess plasma kinin forming activity (kininogenases) and plasma kinin destroying activity (kininases) in varying degrees.2. The common bile duct, especially its lower part, had high kininase activity.3. The liver possessed a high kininase activity, but no kinin forming activity.4. The inactive precursor of plasma kinin, kininogen, was not detected in the bile.5. Results from different pathological conditions are reported.6. The implications of the findings are discussed. Special importance is attached to the question of a formation of kininogenases in the liver and to the significance of a plasma kinin activity in the bile and the biliary tract.
摘要
  1. 人胆汁以及胆道黏膜组织匀浆具有不同程度的血浆激肽形成活性(激肽原酶)和血浆激肽破坏活性(激肽酶)。

  2. 胆总管,尤其是其下段,具有较高的激肽酶活性。

  3. 肝脏具有较高的激肽酶活性,但无激肽形成活性。

  4. 在胆汁中未检测到血浆激肽的无活性前体激肽原。

  5. 报告了不同病理状况的结果。

  6. 讨论了研究结果的意义。特别重视肝脏中激肽原酶形成的问题以及胆汁和胆道中血浆激肽活性的意义。

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本文引用的文献

2
The estimation of urinary kallkrein.尿激肽释放酶的测定
J Physiol. 1959 Oct;148(2):267-82. doi: 10.1113/jphysiol.1959.sp006287.
3
KININ-FORMING AND DESTROYING ACTIVITIES OF SALIVA.唾液的激肽形成和破坏活性
Br J Pharmacol Chemother. 1964 Dec;23(3):440-4. doi: 10.1111/j.1476-5381.1964.tb01600.x.
4
A STABLE SUBSTRATE FOR THE ASSAY OF PLASMA KININ-FORMING ENZYMES.用于测定血浆激肽形成酶的稳定底物。
Br J Pharmacol Chemother. 1963 Dec;21(3):500-8. doi: 10.1111/j.1476-5381.1963.tb02018.x.
5
RELEASE OF A KININ PEPTIDE IN THE CARCINOID SYNDROME.类癌综合征中激肽肽的释放。
Lancet. 1964 Mar 7;1(7332):514-7. doi: 10.1016/s0140-6736(64)92907-1.
6
Kinin-forming and destroying activities of cell homogenates.细胞匀浆的激肽形成和破坏活性。
J Physiol. 1965 Aug;179(3):479-88. doi: 10.1113/jphysiol.1965.sp007674.
7
Separation of 2 different substrates for plasma kinin-forming enzymes.
Nature. 1966 Apr 2;210(5031):98-9. doi: 10.1038/210098a0.

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