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某些脊椎动物物种中修饰糖蛋白的肝脏结合。

Hepatic binding of modified glycoproteins in some species of vertebrates.

作者信息

Dobryszycka W, Osada J, Chorazyczewski J

出版信息

Comp Biochem Physiol B. 1982;71(2):259-63. doi: 10.1016/0305-0491(82)90251-6.

Abstract
  1. Binding activities of hepatic extracts of the rat, chicken, frog and fish for 125I-labeled asialo-, agalacto-, and aN-acetylglucosamino-derivatives of orosomucoid and haptoglobin, were determined. 2. Hepatic receptors of the rat were found to bind preferably asialo-derivatives, those of the chicken agalacto-ones. 3. Hepatic receptors of lower vertebrates showed much lower affinity, in the case of the frog for all the modified glycoproteins whereas in the case of the fish with the exception of aN-acetylglucosamino-derivatives which were not bound at all. 4. Specific binding of derivatives of orosomucoid was higher than that of haptoglobin but equal in terms of molarity.
摘要
  1. 测定了大鼠、鸡、蛙和鱼的肝脏提取物对125I标记的类粘蛋白和触珠蛋白的去唾液酸、去半乳糖和N-乙酰氨基葡萄糖衍生物的结合活性。2. 发现大鼠的肝脏受体优先结合去唾液酸衍生物,鸡的肝脏受体优先结合去半乳糖衍生物。3. 低等脊椎动物的肝脏受体亲和力低得多,蛙的肝脏受体对所有修饰糖蛋白的亲和力都低,而鱼的肝脏受体除了完全不结合的N-乙酰氨基葡萄糖衍生物外,对其他修饰糖蛋白的亲和力也低。4. 类粘蛋白衍生物的特异性结合高于触珠蛋白,但按摩尔浓度计算二者相等。

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