Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 2020 Mar 3;10:3927. doi: 10.1038/s41598-020-60802-z

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

© The Author(s) 2020

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

PMC Copyright notice

Quantification of collagen and tissue weights in the three fractions after pancreas dissociation. (A) Graphical representation of experimental procedure. (B) Undissociated, soluble dissociated, and insoluble dissociated fractions were prepared after pancreas dissociation using recombinant Grimontia hollisae collagenase (solid line) or purified Clostridium histolyticum collagenase (dashed line) with thermolysin (0.012 mg/ml). All fractions from collagenase-treated pancreata were hydrolysed by heating at 110 °C with 6 M HCl for 20 hours. Quantification of hydroxyproline content was performed using a 3200 QTRAP mass spectrometer; the collagen weight in each fraction was converted from hydroxyproline values. The total amino acid content of each fraction was measured with a L-8800 amino acid analyser; the tissue weight of each fraction was converted from the total amino acid content.