ArticlePlanta1992
Aspartic proteinase from barley grains is related to mammalian lysosomal cathepsin D.
Article in Planta, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
What it found
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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.
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Who cites it
12 citing papers in PubMed, 108 citations in OpenAlex.
- Defense and Offense Strategies: The Role of Aspartic Proteases in Plant-Pathogen Interactions.Biology · 2021Review
- Interspecific proteomic comparisons reveal ash phloem genes potentially involved in constitutive resistance to the emerald ash borer.PloS one · 2011Article
- Cardosins in postembryonic development of cardoon: towards an elucidation of the biological function of plant aspartic proteinases.Protoplasma · 2008Article
- Delimitation of the rice wide compatibility gene S5 ( n ) to a 40-kb DNA fragment.TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik · 2005Article
- Review
- A vacuolar sorting domain may also influence the way in which proteins leave the endoplasmic reticulum.The Plant cell · 2001Article
- Programmed cell death in cereal aleurone.Plant molecular biology · 2000Review
- Plant proteolytic enzymes: possible roles during programmed cell death.Plant molecular biology · 2000Review
- Aspartic proteinase genes in the Brassicaceae Arabidopsis thaliana and Brassica napus.Plant molecular biology · 1997Article
- Article
- Purification and partial characterization of a 31-kDa cysteine endopeptidase from germinated barley.Planta · 1996Article
- Ethylene regulates the expression of a cysteine proteinase gene during germination of chickpea (Cicer arietinum L.).Plant molecular biology · 1994Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Resting barley (Hordeum vulgare L.) grains contain acid-proteinase activity. The corresponding enzyme was purified from grain extracts by affinity chromatography on a pepstatin-Sepharose column. The pH optimum of the affinity-purified enzyme was between 3.5 and 3.9 as measured by hemoglobin hydrolysis and the enzymatic activity was completely inhibited by pepstatin a specific inhibitor of aspartic proteinases (EC 3.4.23). Further purification on a Mono S column followed by activity measurements and sodium dodecyl sulfate-polyacrylamide gel electrophoresis revealed that the affinity-purified enzyme preparation contained two active heterodimeric aspartic proteinases: a larger 48k Da enzyme, consisting of 32-kDa and 16-kDa subunits and a smaller one of 40 kDa, consisting of 29-kDa and 11-kDa subunits. Separation and partial amino acid sequence analysis of each subunit indicate that the 40-kDa enzyme is formed by proteolytic processing of the 48k Da form. Amino-acid sequence alignment and inhibition studies showed that the barley aspartic proteinase resembles mammalian lysosomal cathepsin D (EC 3.4.23.5).
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.