ArticleThe Histochemical journal1993
Estimating the initial reaction velocity of a soluble dehydrogenase in situ.
Article in The Histochemical journal, 1993. 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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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.
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Who cites it
8 citing papers in PubMed, 10 citations in OpenAlex.
- Effects of ischaemia and reperfusion on NADH coenzyme Q reductase activity in rat liver.The Histochemical journal · 1999Article
- Analysis of enzyme reactions in situ.The Histochemical journal · 1995Review
- Quantitative comparison between the gel-film and polyvinyl alcohol methods for dehydrogenase histochemistry reveals different intercellular distribution patterns of glucose-6-phosphate and lactate dehydrogenases in mouse liver.The Histochemical journal · 1994Article
- The initial reaction velocities of lactate dehydrogenase in various cell types.The Histochemical journal · 1994Article
- The diverse Michaelis constants and maximum velocities of lactate dehydrogenase in situ in various types of cell.The Histochemical journal · 1994Article
- Estimating the initial reaction velocity of a soluble dehydrogenase in situ.The Histochemical journal · 1993Article
- Kinetic analysis of lactate dehydrogenase in situ in mouse liver determined with a quantitative histochemical technique.The Histochemical journal · 1993Article
- Initial reaction kinetics of succinate dehydrogenase in mouse liver studied with a real-time image analyser system.Histochemistry · 1992Article
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
The initial reaction velocities (vi) of lactate dehydrogenase in single hepatocytes were determined, by microdensitometry or computer-assisted image analysis, in sections of unfixed mouse liver incubated at 37 degrees C on substrate-containing agarose gel films. They were found to fit the equations vi = 2.82 degrees A and vi = vi + 2 degrees A, where vi and degrees A are, respectively, the gradients (or steady-state linear velocities) and the intercepts on the absorbance axis of the linear regression lines of the absorbance (A) on incubation time plots for incubation times between 1 and 3 min. Both equations were independent of section thickness between 4 and 14 microns. The observed and calculated values of vi agreed within 11.5% (n = 71). The validity of the equations for vi was confirmed by showing that the calculated vi was proportional to the thickness of the section and hence the amount of enzyme present. Thus, vi can be determined from measurements of either degrees A alone or vi and degrees A.
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Registered trials
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