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 residue 132. The fragment retains the ability to inhibit activated interstitial collagenase and to block the autocatalytic activation of procollagenase.
DeClerck
Y A
YA
Division of Hematology/Oncology, Childrens Hospital, Los Angeles, CA 90027.
Yean
T D
TD
Lee
Y
Y
Tomich
J M
JM
Langley
K E
KE
D000595:Amino Acid Sequence; D000818:Animals; D016466:CHO Cells; D002417:Cattle; D002851:Chromatography, High Pressure Liquid; D017364:Collagenases / Q000378:metabolism; D006224:Cricetinae; D004591:Electrophoresis, Polyacrylamide Gel; D004789:Enzyme Activation; D004792:Enzyme Precursors / Q000378:metabolism; D008666:Metalloendopeptidases / Q000037:antagonists & inhibitors*; D008969:Molecular Sequence Data; D009363:Neoplasm Proteins / Q000737:chemistry*; D010446:Peptide Fragments / Q000737:chemistry; D051381:Rats; D019716:Tissue Inhibitor of Metalloproteinase-2; D014357:Trypsin
D004792:Enzyme Precursors; D009363:Neoplasm Proteins; D010446:Peptide Fragments; D019716:Tissue Inhibitor of Metalloproteinase-2; D014357:Trypsin; D017364:Collagenases; D008666:Metalloendopeptidases; C022440:procollagenase