Detection of endoproteinases in polyacrylamide gels

Gary R. Petersen, James L. Van Etten

Research output: Contribution to journalArticle

1 Citation (Scopus)

Abstract

A simple and versatile method was developed for detecting endoproteinases by nondenaturing polyacrylamide gel electrophoresis. A vertical strip of the resolving gel is subjected horizontally to a second electrophoresis in the presence of a substrate protein and sodium dodecyl sulfate (SDS). The location of proteolytic activity in the original gel strip is revealed by the disappearance of substrate and the appearance of proteolytic products (due to limited proteolysis) in the second gel. The pattern of peptide fragments produced permits the identification of the protease responsible.

Original languageEnglish (US)
Pages (from-to)433-435
Number of pages3
JournalELECTROPHORESIS
Volume4
Issue number6
DOIs
StatePublished - Feb 1983

Fingerprint

Gels
Electrophoresis
Proteolysis
Peptide Fragments
Substrates
Sodium Dodecyl Sulfate
Polyacrylamide Gel Electrophoresis
Peptide Hydrolases
polyacrylamide gels
Proteins

ASJC Scopus subject areas

  • Analytical Chemistry
  • Biochemistry
  • Clinical Biochemistry

Cite this

Detection of endoproteinases in polyacrylamide gels. / Petersen, Gary R.; Van Etten, James L.

In: ELECTROPHORESIS, Vol. 4, No. 6, 02.1983, p. 433-435.

Research output: Contribution to journalArticle

Petersen, Gary R. ; Van Etten, James L. / Detection of endoproteinases in polyacrylamide gels. In: ELECTROPHORESIS. 1983 ; Vol. 4, No. 6. pp. 433-435.
@article{272a823cbf954425bcc823f6b74ef64b,
title = "Detection of endoproteinases in polyacrylamide gels",
abstract = "A simple and versatile method was developed for detecting endoproteinases by nondenaturing polyacrylamide gel electrophoresis. A vertical strip of the resolving gel is subjected horizontally to a second electrophoresis in the presence of a substrate protein and sodium dodecyl sulfate (SDS). The location of proteolytic activity in the original gel strip is revealed by the disappearance of substrate and the appearance of proteolytic products (due to limited proteolysis) in the second gel. The pattern of peptide fragments produced permits the identification of the protease responsible.",
author = "Petersen, {Gary R.} and {Van Etten}, {James L.}",
year = "1983",
month = "2",
doi = "10.1002/elps.1150040613",
language = "English (US)",
volume = "4",
pages = "433--435",
journal = "Electrophoresis",
issn = "0173-0835",
publisher = "Wiley-VCH Verlag",
number = "6",

}

TY - JOUR

T1 - Detection of endoproteinases in polyacrylamide gels

AU - Petersen, Gary R.

AU - Van Etten, James L.

PY - 1983/2

Y1 - 1983/2

N2 - A simple and versatile method was developed for detecting endoproteinases by nondenaturing polyacrylamide gel electrophoresis. A vertical strip of the resolving gel is subjected horizontally to a second electrophoresis in the presence of a substrate protein and sodium dodecyl sulfate (SDS). The location of proteolytic activity in the original gel strip is revealed by the disappearance of substrate and the appearance of proteolytic products (due to limited proteolysis) in the second gel. The pattern of peptide fragments produced permits the identification of the protease responsible.

AB - A simple and versatile method was developed for detecting endoproteinases by nondenaturing polyacrylamide gel electrophoresis. A vertical strip of the resolving gel is subjected horizontally to a second electrophoresis in the presence of a substrate protein and sodium dodecyl sulfate (SDS). The location of proteolytic activity in the original gel strip is revealed by the disappearance of substrate and the appearance of proteolytic products (due to limited proteolysis) in the second gel. The pattern of peptide fragments produced permits the identification of the protease responsible.

UR - http://www.scopus.com/inward/record.url?scp=0021046077&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0021046077&partnerID=8YFLogxK

U2 - 10.1002/elps.1150040613

DO - 10.1002/elps.1150040613

M3 - Article

AN - SCOPUS:0021046077

VL - 4

SP - 433

EP - 435

JO - Electrophoresis

JF - Electrophoresis

SN - 0173-0835

IS - 6

ER -