兔补体第一成分亚组分Clq的结构与活性研究。
Studies on the structure and activity of rabbit Clq (a subcomponent of the first component of complement).
作者信息
Lowe D M, Reid K B
出版信息
Biochem J. 1974 Nov;143(2):265-72. doi: 10.1042/bj1430265.
Abstract
- The subunit structure of rabbit subcomponent C1q was examined in a previous publication (Reid et al., 1972). The present paper describes some aspects of the structure of the polypeptide chains derived from the molecule. 2. The three polypeptide chains, produced by performic oxidation, of rabbit subcomponent C1q were isolated by ion-exchange chromatography in 8m-urea on DEAE-cellulose. 3. Each chain was found to contain 15-18% glycine and significant amounts of the amino acids hydroxyproline and hydroxylysine. 4. By means of collagenase digestion it was shown that all three chains of rabbit subcomponent C1q contain collagen-like sequences of amino acids which constitute about 40% of each chain. 5. By use of carboxypeptidase A it was established, indirectly, that the collagen-like sequences, in one of the chains, are probably located near, or at, the N-terminal end of the chain. 6. Collagenase digestion and heating at 52 degrees C (but not at 49 degrees C) caused rapid loss of native rabbit subcomponent C1q haemolytic activity.
摘要
- 兔补体亚成分C1q的亚基结构已在先前的一篇文献中进行了研究（Reid等人，1972年）。本文描述了源自该分子的多肽链结构的一些方面。2. 通过过甲酸氧化产生的兔补体亚成分C1q的三条多肽链，在8M尿素中于DEAE-纤维素上通过离子交换色谱法进行分离。3. 发现每条链含有15%-18%的甘氨酸以及大量的氨基酸羟脯氨酸和羟赖氨酸。4. 通过胶原酶消化表明，兔补体亚成分C1q的所有三条链都含有氨基酸的胶原样序列，这些序列约占每条链的40%。5. 通过使用羧肽酶A间接确定，其中一条链中的胶原样序列可能位于链的N端附近或N端。6. 胶原酶消化和在52℃（而非49℃）加热导致天然兔补体亚成分C1q溶血活性迅速丧失。
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