ArticleJournal of protein chemistry1994
Isolation and characterization of octopus hepatopancreatic glutathione S-transferase. Comparison of digestive gland enzyme with lens S-crystallin.
Article in Journal of protein chemistry, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 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
8 citing papers in PubMed, 32 citations in OpenAlex.
- Evolution and development of complex eyes: a celebration of diversity.Development (Cambridge, England) · 2020Review
- Structure of a Highly Active Cephalopod S-crystallin Mutant: New Molecular Evidence for Evolution from an Active Enzyme into Lens-Refractive Protein.Scientific reports · 2016Article
- Inhibition of octopus glutathione transferase by Meisenheimer complex analog, S-(2,4,6-trinitrophenyl) glutathione.Journal of protein chemistry · 2000Article
- Molecular basis for the polymerization of octopus lens S-crystallin.Biophysical journal · 2000Article
- Homology modeling of cephalopod lens S-crystallin: a natural mutant of sigma-class glutathione transferase with diminished endogenous activity.Biophysical journal · 1999Article
- Kinetic mechanism of octopus hepatopancreatic glutathione transferase in reverse micelles.The Biochemical journal · 1996Article
- Glutathione S-transferase and S-crystallins of cephalopods: evolution from active enzyme to lens-refractive proteins.Journal of molecular evolution · 1995Article
- Steady-state kinetics and chemical mechanism of octopus hepatopancreatic glutathione transferase.The Biochemical journal · 1995Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Glutathione S-transferase from Octopus vulgaris hepatopancreas was purified to apparent homogeneity by single glutathione-Sepharose-4B affinity chromatography with overall yield 46% and purification 249-fold. The enzyme was a homodimer with subunit M(r) 24,000, which was smaller than that of the octopus lens S-crystallin (M(r) 27,000) with glutathione-S-transferase-like structure. Both proteins showed substrate specificities similar to alpha/pi-type isozyme of glutathione S-transferase. Under native conditions, both proteins exhibited multiple forms upon polyacrylamide gel electrophoresis or isoelectric focusing, albeit with distinct mobilities; however, only one kind of N-terminal amino acid sequence was determined for the multiple forms of each protein. The hepatopancreatic GST, with pI value 6.6-7.3, dissociated into two monomers in an acidic or alkaline environment. Two amino acid residues, with pKa values 5.69 +/- 0.14 and 9.03 +/- 0.11 were involved in the subunit interactions of the hepatopancreatic enzyme.
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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.