Xia Y, Garcia G, Chen S, Wilson C B, Feng L
Department of Immunology, The Scripps Research Institute, La Jolla, CA 92037, USA.
FEBS Lett. 1996 Mar 18;382(3):285-8. doi: 10.1016/0014-5793(96)00185-8.
A full-length cDNA for rat 92-kDa type IV collagenase was isolated and sequenced. RNase protection assay revealed tissue specific differential expression of the 92-kDa type IV collagenase in the rat during development. Natural and modified forms of the 92-kDa type IV collagenase were expressed. One active protein, 92-CD, contained only the putative catalytic domain. Large quantities of the 92-CD were expressed in Escherichia coli, extracted from inclusion bodies, purified, and refolded to an active form. This recombinant protein was able to cleave denatured and native collagen and was inactivated by known MMP inhibitors.
分离并测序了大鼠92 kDa IV型胶原酶的全长cDNA。核糖核酸酶保护试验揭示了92 kDa IV型胶原酶在大鼠发育过程中的组织特异性差异表达。表达了92 kDa IV型胶原酶的天然形式和修饰形式。一种活性蛋白92-CD仅包含推定的催化结构域。大量的92-CD在大肠杆菌中表达，从包涵体中提取、纯化并重折叠成活性形式。这种重组蛋白能够切割变性和天然胶原蛋白，并被已知的基质金属蛋白酶抑制剂灭活。
