ArticleACS measurement science au2025
Measuring Thiaminase Activity in Fish Extracts using Fluorescence Spectrophotometry.
Article in ACS measurement science au, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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
0 citing papers in PubMed.
No citing paper in PubMed yet.
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.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Thiaminase is an enzyme that destroys thiamine (vitamin B1) and is present in various fishes, mussels, plants, and bacteria. A sensitive and versatile assay is needed to measure thiaminase activity in complex biological samples using common reagents and variable reaction conditions. We developed a simple assay that uses fluorescence spectrophotometry and a microplate reader to measure thiaminase activity in fish tissue extracts via the destruction of added thiamine over time. Thiamine concentration, cosubstrate choice and concentration, and pH can be varied according to the needs of the investigator. Using this assay, we successfully measured common enzyme kinetic constants for thiaminase from a Pacific herring extract. The enzyme exhibited Michaelis-Menten kinetics (
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.