Purification and Characterisation of Human 72-kDa Gelatinase (Type IV Collagenase). Use of Immunolocalisation to Demonstrate the Non-coordinate Regulation of the 72-kDa and 95-kDa Gelatinases by Human Fibroblasts-Reference-Cited by-同舟云学术

Purification and Characterisation of Human 72-kDa Gelatinase (Type IV Collagenase). Use of Immunolocalisation to Demonstrate the Non-coordinate Regulation of the 72-kDa and 95-kDa Gelatinases by Human Fibroblasts

Published:1991-01 Issue:1 Volume:372 Page:287-296
ISSN:0177-3593
Container-title:Biological Chemistry Hoppe-Seyler
language:en
Short-container-title:Biological Chemistry Hoppe-Seyler

Author:

HIPPS Deborah S.,HEMBRY Rosalind M.,DOCHERTY Andrew J. P.,REYNOLDS John J.,MURPHY Gillian

Publisher

Walter de Gruyter GmbH

Subject

Biochemistry

Link

https://www.degruyter.com/document/doi/10.1515/bchm3.1991.372.1.287/pdf

Reference26 articles.

1. Purification and characterization of a bone metalloproteinase that degrades gelatin and types IV and V collagen

2. H-ras oncogene-transformed human bronchial epithelial cells (TBE-1) secrete a single metalloprotease capable of degrading basement membrane collagen.

3. Purification and properties of a gelatin-specific neutral protease from human skin.

4. ‘Gelatinase-like’ activity from articular chondrocytes in monolayer culture

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