title: Characterization of the functional domain of tissue inhibitor of metalloproteinases-2 (TIMP-2).
abstract: 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.
authors.affiliation: Division of Hematology/Oncology, Childrens Hospital, Los Angeles, CA 90027.
authors.forename: Y A
authors.initials: YA
authors.lastname: DeClerck
authors.forename: T D
authors.initials: TD
authors.lastname: Yean
authors.forename: Y
authors.initials: Y
authors.lastname: Lee
authors.forename: J M
authors.initials: JM
authors.lastname: Tomich
authors.forename: K E
authors.initials: KE
authors.lastname: Langley
mesh_terms: 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
chemical_list: D004792:Enzyme Precursors; D009363:Neoplasm Proteins; D010446:Peptide Fragments; D019716:Tissue Inhibitor of Metalloproteinase-2; D014357:Trypsin; D017364:Collagenases; D008666:Metalloendopeptidases; C022440:procollagenase