Steffen C, Timpl R, Wolff I, Furthmayr H
Immunology. 1970 Jun;18(6):849-54.
Serologically active collagen peptides obtained after trypsin or collagenase treatment were further digested by different proteases. The influence of degradation on the inhibiting activity was studied with collagen antibodies possessing three different restricted specificities. Structures responsible for general collagen specificity proved to be highly resistant to the action of different proteases except for collagenase. This suggests the location of this specificity in the helical apolar sequences of collagen. Quite in contrast species-specific structures appeared very susceptible to the further degradations used.
经胰蛋白酶或胶原酶处理后获得的具有血清学活性的胶原肽,再用不同的蛋白酶进一步消化。用具有三种不同受限特异性的胶原抗体研究了降解对抑制活性的影响。除胶原酶外,负责一般胶原特异性的结构对不同蛋白酶的作用具有高度抗性。这表明这种特异性位于胶原的螺旋非极性序列中。相比之下,物种特异性结构对所用的进一步降解显得非常敏感。