IDENTIFICATION OF SITES IN COLLAGEN ALPHA-CHAINS THAT BIND SERUM ANTI-GELATIN FACTOR (COLD-INSOLUBLE GLOBULIN)
IDENTIFICATION OF SITES IN COLLAGEN ALPHA-CHAINS THAT BIND SERUM ANTI-GELATIN FACTOR (COLD-INSOLUBLE GLOBULIN)
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DOI：
10.1042/bj1690055
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发表时间：
1978-01-01
影响因子：
4.1
通讯作者：
MARTIN, GR
中科院分区：
文献类型：
--
作者：
DESSAU, W;ADELMANN, BC;MARTIN, GR
用变性Ⅰ型胶原亲和层析法从豚鼠和人血清中制备抗明胶因子。在抑制试验中，观察到天然和变性I、II、III和IV型胶原的活性相当。不同种属的胶原蛋白之间的反应性也没有差异。胶原蛋白α-胶原蛋白中的反应位点通过对不同的CNBr和胶原酶衍生肽的抑制测定来定位链。用α 1（I）-、α 2-和α 1（II）-链的片段获得的结果表明，最具活性的区域位于α 1-链的643和819位之间。发现胶原蛋白的其它区域的活性较低，这可能表明该因子具有与α-胶原蛋白中的几个位点相互作用的潜力。店
Anti-gelatin factor was prepared from guinea-pig and human serum by affinity chromatography on denatured type-I collagen. In the inhibition assay comparable activities were observed for native and denatured type-I, -II, -III and -IV collagens. There was also no difference in reactivity between collagens of different species. The reactive sites in the collagen .alpha.-chains were located by inhibition assays on distinct CNBr- and collagenase-derived peptides. The results obtained with fragments from .alpha.1(I)-, .alpha.2- and .alpha.1(II)-chains indicate that the most active region is located between positions 643 and 819 of the .alpha.1-chain. Lower activities were found for other regions of collagen and may indicate that the factor has the potential to interact with several sites in the .alpha.-chains.