The recombinant catalytic domain of mouse collagenase-3 depolymerizes type I collagen by cleaving its aminotelopeptides.
The recombinant catalytic domain of mouse collagenase-3 depolymerizes type I collagen by cleaving its aminotelopeptides.
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小鼠胶原酶 3 的重组催化结构域通过裂解其氨基肽来解聚 I 型胶原。
DOI：
10.1006/bbrc.1996.5924
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发表时间：
1997
影响因子：
3.1
通讯作者：
Y. Eeckhout
中科院分区：
文献类型：
--
作者：
V. Lemaître;A. Jungbluth;Y. Eeckhout
用聚合酶链反应扩增小鼠胶原酶-3（MMP-13）催化结构域的编码序列，并在大肠杆菌中表达。主要以包涵体形式回收的重组催化结构域（CCD）经复性和制备性SDS-PAGE纯化至均一。纯化的CCD降解明胶，酪蛋白和合成肽。CCD不能切割I型胶原的三螺旋结构域，但保留了全长胶原酶-3切割N-端肽的特异性。这些结果表明，参与识别和切割的氨基端肽的I型胶原蛋白的残基位于小鼠胶原酶-3的催化结构域和C-末端结构域是不需要这种活性。
The sequence coding for the catalytic domain of mouse collagenase-3 (MMP-13) was amplified by polymerase chain reaction and expressed in Escherichia coli. The recombinant catalytic domain (CCD), mainly recovered as inclusion bodies, was renatured and purified to homogeneity by preparative SDS-PAGE. The purified CCD degraded gelatin, casein and a synthetic peptide. CCD was not able to cleave the triple-helical domain of type I collagen but conserved the specific property of full-length collagenase-3 to cleave the N-telopeptides. These results show that residues involved in the recognition and cleavage of the aminotelopeptides of type I collagen are located in the catalytic domain of mouse collagenase-3 and that the C-terminal domain is not required for this activity.
DOI：
--
发表时间：
1990
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
Quinn,CO;Scott,DK;Brinckerhoff,CE;Matrisian,LM;Jeffrey,JJ;Partridge,NC
通讯作者：
Partridge,NC
DOI：
10.1042/bj2910847
发表时间：
1993
期刊：
The Biochemical journal
影响因子：
--
作者：
Knäuper,V;Osthues,A;DeClerck,YA;Langley,KE;Bläser,J;Tschesche,H
通讯作者：
Tschesche,H