phenylmercuric-acetate and Thyroid-Neoplasms

phenylmercuric-acetate has been researched along with Thyroid-Neoplasms* in 1 studies

Other Studies

1 other study(ies) available for phenylmercuric-acetate and Thyroid-Neoplasms

Article	Year
Purification of aminophenyl mercuryacetate-activated human matrix metalloproteinase 1 and removal of the organomercurial in a single-step chromatography. Bioseparation, 1999, Volume: 7, Issue:6 Matrix metalloproteinases are secreted from different cells as inactive zymogens. For their activation in vitro organomercurials may be used, the presence of which, however, can falsify activity assays and modulate the effects of the proteases in subsequent investigations. Here, we demonstrate the binding of human matrix metalloproteinase 1 to a thiophilic resin (mercaptoethylquinazolinedione derivatized agarose) and take advantage of this thiophilic interaction for the purification of organomercurial activated matrix metalloproteinase 1 from the supernatant of a thyroid carcinoma cell line in connection with the simultaneous removal of the activator. Topics: Chromatography, Affinity; Culture Media; Electrophoresis, Polyacrylamide Gel; Enzyme Activation; Humans; Matrix Metalloproteinase 1; Phenylmercuric Acetate; Substrate Specificity; Sulfhydryl Reagents; Thyroid Neoplasms; Tumor Cells, Cultured	1999

Article

Year

Purification of aminophenyl mercuryacetate-activated human matrix metalloproteinase 1 and removal of the organomercurial in a single-step chromatography.

Bioseparation, 1999, Volume: 7, Issue:6

Matrix metalloproteinases are secreted from different cells as inactive zymogens. For their activation in vitro organomercurials may be used, the presence of which, however, can falsify activity assays and modulate the effects of the proteases in subsequent investigations. Here, we demonstrate the binding of human matrix metalloproteinase 1 to a thiophilic resin (mercaptoethylquinazolinedione derivatized agarose) and take advantage of this thiophilic interaction for the purification of organomercurial activated matrix metalloproteinase 1 from the supernatant of a thyroid carcinoma cell line in connection with the simultaneous removal of the activator.

Topics: Chromatography, Affinity; Culture Media; Electrophoresis, Polyacrylamide Gel; Enzyme Activation; Humans; Matrix Metalloproteinase 1; Phenylmercuric Acetate; Substrate Specificity; Sulfhydryl Reagents; Thyroid Neoplasms; Tumor Cells, Cultured

1999