ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

A neutral collagenase from human gastric mucosa | JoVE Visualize

Home
Research Domains
Engineering

A neutral collagenase from human gastric mucosa

D E Woolley, J S Tucker, G Green

The Biochemical Journal|January 1, 1976

View abstract on PubMed

Summary

Human gastric mucosa releases a collagen-degrading enzyme essential for tissue repair. This neutral collagenase enzyme exhibits specific characteristics, including its molecular weight and cleavage site on collagen molecules.

Area of Science:

Biochemistry
Molecular Biology
Gastroenterology

Background:

Human gastric mucosa in culture releases enzymes.
Collagen degradation is crucial for tissue remodeling.

Purpose of the Study:

To characterize a collagen-degrading enzyme from human gastric mucosa.
To determine the enzyme's properties and compare it to known collagenases.

Main Methods:

Culturing human gastric biopsy specimens.
Enzyme activity assays on undenatured collagen.
Gel filtration and electron microscopy for characterization.

Main Results:

A collagenase was isolated, with peak activity after 2-3 days.
The enzyme cleaved collagen between bands 43 and 44, producing specific fragments.
Optimal activity was at pH 7.5-8.5; molecular weight approx. 38000 Da.
Inhibited by alpha2-macroglobulin and EDTA, but not alpha1-antitrypsin.

Conclusions:

Human gastric mucosa produces a neutral collagenase.
The enzyme's molecular size and collagen cleavage site differ from other characterized collagenases.

Chemical Engineering

Reaction Engineering (excl. Nuclear Reactions)

A Neutral Collagenase From Human Gastric Mucosa