Accelerated trypsin autolysis by affinity polymer templates-Reference-Cited by-同舟云学术

Accelerated trypsin autolysis by affinity polymer templates

Published:2020 Issue:48 Volume:10 Page:28711-28719
ISSN:2046-2069
Container-title:RSC Advances
language:en
Short-container-title:RSC Adv.

Author:

Smolin Daniel¹²³⁴,Tötsch Niklas⁵²³⁴^ORCID,Grad Jean-Noël⁵²³⁴^ORCID,Linders Jürgen¹²³⁴,Kaschani Farnusch⁵²³⁴,Kaiser Markus⁵²³⁴^ORCID,Kirsch Michael⁶⁷⁴^ORCID,Hoffmann Daniel⁵²³⁴^ORCID,Schrader Thomas¹²³⁴^ORCID

Affiliation:

1. Faculty of Chemistry

2. University of Duisburg-Essen

3. 45117 Essen

4. Germany

5. Faculty of Biology

6. University Clinics

7. Essen

Abstract

Affinity copolymers specifically recognize the trypsin surface and act as templates for multiple protease molecules, leading to drastically accelerated autolysis – an unusual way for highly efficient enzyme inhibition at physiological conditions.

Funder

Deutsche Forschungsgemeinschaft

Publisher

Royal Society of Chemistry (RSC)

Subject

General Chemical Engineering,General Chemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2020/RA/D0RA05827K

Reference34 articles.

1. Hereditary pancreatitis is caused by a mutation in the cationic trypsinogen gene

2. Inhibition and accelerated autolysis of trypsin due to incorporation of polymer of oxidized methyl linolenate.

3. The N- and C-terminal autolytic fragments of CAPN3/p94/calpain-3 restore proteolytic activity by intermolecular complementation

4. Enhancement of thermostability and resistance against autolysis in a zinc metalloprotease

5. The influence of copper on alkaline protease stability toward autolysis and thermal inactivation

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