ArticleThe Biochemical journal1996
Expression of soluble cloned porcine pepsinogen A in Escherichia coli.
Article in The Biochemical journal, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
6 citing papers in PubMed, 35 citations in OpenAlex.
- Crystal structures of the free and inhibited forms of plasmepsin I (PMI) from Plasmodium falciparum.Journal of structural biology · 2011Article
- Strategies for successful recombinant expression of disulfide bond-dependent proteins in Escherichia coli.Microbial cell factories · 2009Article
- Cloning of the authentic bovine gene encoding pepsinogen a and its expression in microbial cells.Applied and environmental microbiology · 2004Article
- Construction, expression and characterization of a chimaeric mammalian-plant aspartic proteinase.The Biochemical journal · 2003Article
- Identification of copper ligands in Aspergillus oryzae tyrosinase by site-directed mutagenesis.The Biochemical journal · 2000Article
- The pepsin residue glycine-76 contributes to active-site loop flexibility and participates in catalysis.The Biochemical journal · 2000Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A system for the production of soluble porcine pepsinogen A (EC 3.4.23.1) was developed by fusing the pepsinogen and thioredoxin genes and then expressing the fused product (Trx-PG) in Escherichia coli. The expressed fusion protein was purified using a combination of ion-exchange and hydrophobic chromatography. Trypsin digestion of the fusion protein yielded pepsinogen which was one residue longer than the intrinsic length. Acidification of either the fusion protein or pepsinogen (tryptic digestion of Trx-PG) yielded recombinant pepsin A (r-pepsin). When compared with commercial porcine pepsin A, r-pepsin had similar milk-clotting and proteolytic activities, kinetic parameters and pH dependency. The above results indicate that an expression system was developed which yielded fully active soluble pepsin(ogen) from Escherichia coli.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.