The guinea pig pancreas secretes a single trypsinogen isoform, which is defective in autoactivation.

ABSTRACT:

Objectives

The aim of the present study was to purify and clone the trypsinogen isoforms from the guinea pig pancreas and characterize their activation properties.

Methods

Trypsinogens from pancreatic homogenates were isolated by ecotin-affinity chromatography, followed by cation-exchange chromatography. Activation of trypsinogens was tested with enteropeptidase, cathepsin B, and trypsin. Complementary DNAs for pretrypsinogens were cloned from total RNA after reverse transcription and polymerase chain reaction amplification.

Results

Purification of trypsinogens yielded a single peak with an N-terminal amino-acid sequence of LPIDD. Cloning of pretrypsinogen cDNAs revealed 2 distinct but nearly identical isoforms. At the amino acid level, the only difference between the

SUBMITTER: Ozsvari B 

PROVIDER: S-EPMC2708092 | biostudies-literature | 2008 Aug

REPOSITORIES: biostudies-literature