Monboisse J C, Bellon G, Dufer J, Randoux A, Borel J P
Laboratory of Biochemistry, CNRS UA 610, UFR Medicine, Reims, France.
Biochem J. 1987 Sep 15;246(3):599-603. doi: 10.1042/bj2460599.
Human polymorphonuclear neutrophils (PMNs), purified on Ficoll-Hypaque cushions, were incubated for 5 min with calf skin acid-soluble collagen and the released superoxide anions (O2-) measured spectrophotometrically by reduction of ferricytochrome c or by chemiluminescence analysis. This collagen stimulated the release of O2- unless it had been treated with pepsin. The stimulatory activity remained in denatured collagen, was contained only in the alpha 1(I) chain and was present in the alpha 1(I)-CB 6 (CNBr-cleaved) peptide, which is C-terminal. The activity was linearly dependent on the collagen concentration up to about 200 micrograms/ml. In addition, this collagen induced a release of beta-glucuronidase and N-acetyl-beta-glucosaminidase from PMNs.
在Ficoll-Hypaque梯度离心垫层上纯化的人多形核中性粒细胞（PMNs），与小牛皮肤酸溶性胶原蛋白孵育5分钟，然后通过还原铁细胞色素c或化学发光分析，用分光光度法测量释放的超氧阴离子（O2-）。这种胶原蛋白能刺激O2-的释放，除非它已经用胃蛋白酶处理过。刺激活性保留在变性胶原蛋白中，仅存在于α1（I）链中，并且存在于C末端的α1（I）-CB 6（溴化氰裂解）肽中。该活性在胶原蛋白浓度高达约200微克/毫升时呈线性依赖关系。此外，这种胶原蛋白诱导PMNs释放β-葡萄糖醛酸酶和N-乙酰-β-氨基葡萄糖苷酶。
