Characterization of the functional domain of tissue inhibitor of metalloproteinases-2 (TIMP-2)

Analysis of the functional domain of tissue inhibitor of metallo-proteinases-2 (TIMP-2) was performed using limited proteolytic degradation with trypsin. This treatment generated a 13.5 kDa fragment which was purified and shown to consist of an uncleaved N-terminal region extending from residue 1 to...

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Veröffentlicht in:	Biochemical journal 1993, Vol.289 (1), p.65-69
Hauptverfasser:	DECLERCK, Y. A, YEAN, T.-D, LEE, Y, TOMICH, J. M, LANGLEY, K. E
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Analytical, structural and metabolic biochemistry Animals Biological and medical sciences Cattle CHO Cells Chromatography, High Pressure Liquid Collagenases - metabolism Cricetinae Electrophoresis, Polyacrylamide Gel Enzyme Activation Enzyme Precursors - metabolism Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology Hydrolases Metalloendopeptidases - antagonists & inhibitors Molecular Sequence Data Neoplasm Proteins - chemistry Peptide Fragments - chemistry Rats Tissue Inhibitor of Metalloproteinase-2 Trypsin
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Zusammenfassung:	Analysis of the functional domain of tissue inhibitor of metallo-proteinases-2 (TIMP-2) was performed using limited proteolytic degradation with trypsin. This treatment generated a 13.5 kDa fragment which was purified and shown to consist of an uncleaved N-terminal region extending from residue 1 to residue 132. The fragment retains the ability to inhibit activated interstitial collagenase and to block the autocatalytic activation of procollagenase.
ISSN:	0264-6021 1470-8728
DOI:	10.1042/bj2890065